 Patent Application Title |
Patent App Num. |
Date |
 Production and use of bacterial histamine | 20130149291 | 20130613 |
 A method is provided of selecting specific probiotic lactic acid bacteria producing histamine and the use of such strains for beneficial effects for mammals. The method includes selecting a lactic acid bacterial strain for use in the local production of histamine in a mammal, and further comprises screening bacteria for the presence of an. active histidine operon and selecting a strain which has an active histidine operon and is capable of producing histamine. Preferably said strain is selected for its ability to produce histamine at a level of greater than 250 pg/ml. The present invention further provides products comprising the strains obtainable by the selection methods of the invention for use in the local production, of histamine in a mammal, in particular for use in the... |
| Histidine rich protein-2 diagnostic test for cerebral malaria | 20130131104 | 20130523 |
 The present inventions relate to accurately identifying a subset of patients within a larger group with malarial parasitemia. In particular, the present inventions provide compositions and methods comprising a malarial protein, histidine rich pro-tein-2 (HRP-2) for determining the general severity of a malarial infection in patients. Specifically, the inventions provide a rapid test comprising a read-out for HRP-2 levels in bodily fluids for determining whether a comatose patient's disease is a result of malaria as opposed to coma of another cause with incidental parasitemia. Specifically, in one preferred embodiment, a rapid test is contemplated as a quantitative rapid test dipstick. Further, these inventions relate to predictive tests for patients at risk for progression of relatively mild malaria disease to the more life-threatening cerebral malaria in addition... |
| Long-acting insulin analogue preparations in soluble and crystalline forms | 20130085101 | 20130404 |
 A pharmaceutical formulation comprises an insulin analogue or a physiologically acceptable salt thereof, wherein the insulin analogue or a physiologically acceptable salt thereof contains an insulin A-chain sequence that contains paired Histidine substitutions at A4 and A8, and optionally a substitution at A21. The formulation further contains a pharmaceutically acceptable buffer containing at least about 4 zinc ions per 6 insulin analogue molecules. The formulation forms a long-acting zinc-dependent subcutaneous depot upon subcutaneous injection. In a zinc-free formulation, the insulin analogue monomer exhibits decreased affinity for the Insulin-like Growth Factor receptor and at least 20% of the affinity for the insulin receptor of the same species, in comparison to an otherwise identical insulin or insulin analogue that does not contain the HisA4 and HisA8 substitutions.
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| Amyloid precursor protein e2 domain and uses thereof | 20130052654 | 20130228 |
 Members of the Amyloid Precursor Protein family (APP molecules) and their neurotoxic cleavage product Aβ are key players in the development of Alzheimer's disease (AD). Proteolytic processing of APP molecules is influenced by metal ions, protein ligands and its oligomerization state. X-ray structures of the metal bound molecule at 2.6-2.0 Å resolution are presented, providing structural and functional bases for the regulation of APP molecules using conformational information. A metal-dependent molecular switch located within the E2 domain of APP coinciding with a high affinity copper and zinc binding site within the monomeric E2 domain was evaluated. The metal specific coordination spheres of this E2 domain comprise four evolutionary conserved histidine residues. Metal binding induces large conformational changes relative to the metal free protein. This conformational change... |
| Glp-1 analogues and derivatives | 20130053311 | 20130228 |
 The invention relates to a GLP-1 analogue which comprises a histidine (H) residue at a position corresponding to position 31 of GLP-1 (7-37) (SEQ ID NO: 1), a glutamine (Q) residue at a position corresponding to position 34 of GLP-1 (7-37) (SEQ ID NO: 1), and a maximum of ten amino acid modifications as compared to GLP-1 (7-37) (SEQ ID NO: 1); wherein the H residue is designated H31, and the Q residue is designated Q34; or a pharmaceutically acceptable salt, amide, or ester thereof. The invention also relates to derivatives thereof, as well as the pharmaceutical use of these analogues and derivatives, for example in the treatment and/or prevention of all forms of diabetes and related diseases. The invention furthermore relates to corresponding novel side... |
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| Filler for affinity chromatography and method for isolating immunoglobulin | 20130041135 | 20130214 |
| wherein R represents an amino acid sequence consisting of 4 to 300 amino acid residues containing a region consisting of 4 to 20 contiguous histidine residues; and R2 represents an amino acid sequence capable of binding to immunoglobulin, the amino acid sequence consisting of 50 to 500 amino acid residues containing Z domain of Protein A or a fragment thereof, or a variant thereof, provided that the R binds to C-terminus or N-terminus of the R2.
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| Production and use of bacterial histamine | 20130022586 | 20130124 |
| A method is provided of selecting specific probiotic lactic acid bacteria producing histamine and the use of such strains for beneficial effects for mammals. The method includes selecting a lactic acid bacterial strain for use in the local production of histamine in a mammal, and further comprises screening bacteria for the presence of an active histidine operon and selecting a strain which has an active histidine operon and is capable of producing histamine. Preferably said strain is selected for its ability to produce histamine at a level of greater than 250 pg/ml. The present invention further provides products comprising the strains obtainable by the selection methods of the invention for use in the local production of histamine in a mammal, in particular for use in the... |
| Stabilized antibody-containing liquid formulations | 20130022625 | 20130124 |
| The present inventors discovered that a significant stabilization effect was achieved by using an acidic amino acid, aspartic acid or glutamic acid as a counter ion species in histidine buffer or tris(hydroxymethyl)aminomethane, specifically by using histidine-aspartate buffer or histidine-glutamate buffer, or tris(hydroxymethyl)aminomethane-aspartate or tris(hydroxymethyl)aminomethane-glutamate as a buffer. The present inventors also discovered that a significant stabilization effect was achieved by using an acidic amino acid, aspartic acid or glutamic acid, as a counter ion species to a basic amino acid such as arginine, specifically by using arginine-aspartate or arginine-glutamate.
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| Method of producing recombinant tat-hoxb4h protein for use as a stimulant of hematopoiesis in vivo | 20120322979 | 20121220 |
| The present invention relates to a new and nonobvious method of producing the C-terminal histidine tagged TAT-HOXB4 fusion protein (TAT-HOXB4H), providing unexpected benefits of increased yield and stability to allow for in vivo administration of this protein, and pharmaceutical composition comprising an effective ingredient, TAT-HOXB4H, having stimulatory activity on the production of hematopoietic cells. More specifically, recombinant TAT-HOXB4H protein enhances engraftment of bone marrow transplants, hematopoietic reconstruction, bone marrow re-population and number of circulating stem cells, particularly after chemotherapy or irradiation.
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| Sensitization of immune system against haptenized melanoma antigens | 20120315304 | 20121213 |
| The metabolization of certain phenols, monophenols or benzenediols into reactive quinone compounds, in particular ortho-quinones and related reactive intermediates, which is brought about by oxidation of monophenols and benzenediols by proteins exhibiting tyrosinase activity, such as human tyrosinase and the related proteins TRP1 and TRP2. The compounds function as haptens that become covalently bound to the tyrosinase enzymes, in particular to histidine moieties, in or near the catalytic site of proteins exhibiting tyrosinase activity, such as tyrosinase, TRP1 and TRP2. An immune response is then to be mounted against these haptenized auto-antigens to treat malignancies.
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| Substances and methods for the treatment of lysosmal storage diseases | 20120308544 | 20121206 |
| The present invention relates to a chimeric molecule comprising (i) a targeting moiety that binds to heparin or heparan sulfate proteoglycans, (ii) a lysosomal peptide or protein, (iii) wherein the targeting moiety is a neurotrophic growth factor and/or, wherein the targeting moiety comprises one of the following consensus sequences BBXB, BXBB, BBXXB, BXXBB, BBXXXB or BXXXBB and wherein B represents an arginine, lysine or histidine amino acid and X represents any amino acid, (iii) with the proviso that the targeting moiety is at least thirteen amino acids long.
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| Treatment of copd, gastro-esophageal reflux disease (gerd), food allergies and other gastrointestinal conditions and disorders ameliorated by proper histamine management using a combination of histidine decarboxylase inhibators, lra drugs, anti-h1 and/or | 20120295933 | 20121122 |
| The invention provides a method for the treatment of COPD and/or gastrointestinal disease conditions ameliorated by histamine management in a subject, comprising administering to the subject an effective amount of a histidine decarboxylase inhibitor.
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| Methods of purifying viruses using gel permeation chromatography | 20120273424 | 20121101 |
| Provided herein are elution buffers and methods for purifying viruses using gel permeation chromatography. The methods are useful, for example, in increasing recovery of a virus from a gel permeation chromatography column. The buffers for use in the methods include at least one excipient selected from histidine or sucrose, a divalent cation, a non-ionic detergent, and a phosphate buffered saline.
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| Stable formulations of polypeptides and uses thereof | 20120244158 | 20120927 |
| Formulations are provided that contain single variable domains with a good solubility and good stability under different storage, transportation and stress conditions. The formulations are useful as pharmaceutical formulation. The formulation comprises an aqueous carrier with a pH of 5.5 to 8.0, a buffer selected from the group consisting of histidine pH 6.0-6.5, hepes pH 7.0-8.0, MES pH 6.0, succinate pH 6.0-6.5 and acetate pH 5.5-6.0; an excipient; and/or a surfactant selected from Tween 80, Tween 20 and poloxamers. The formulation is further characterized that it has an inorganic salt concentration of 150 mM or lower. The invention further relates to containers and pharmaceutical units comprising such formuSations and to methods for preparing and prophylactic and therapeutic uses of the formulations and pharmaceutical units of the... |
| Pharmaceutical formulation containing immunoglobulin | 20120237532 | 20120920 |
| A set of at least two different protein conjugate preparations, each protein conjugate preparation comprising histidine as a buffering agent and a protein conjugate comprising one or more immunoglobulin moieties conjugated to a carrier protein; wherein the immunoglobulin moieties of each element of said set of protein conjugate preparation have identical complementarity determining regions (CDRs); and wherein different protein conjugate preparations differ in that the immunoglobulin moieties of the protein conjugates have different CDRs.
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| Novel method for quantifying proteins by mass spectrometry | 20120208224 | 20120816 |
| The present invention relates to a method for the quantitative detection of a target protein in a sample, in which the second-generation fragment ions are detected for providing a series of quantitative measurements, at least one of which is correlated to the amount of proteotypic peptide generated and to the amount of target protein in the sample, characterized in that the selected first-generation fragment ion having a mass (m/z)2 is a doubly-charged peptide having a proline and/or a histidine in position 1.
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| Encapsulation of plasmid dna (lipogenes) and therapeutic agents with nuclear localization signal/fusogenic peptide conjugates into targeted liposome complexes | 20120183596 | 20120719 |
| A method is disclosed for encapsulating plasmids, oligonucleotides or negatively-charged drugs into liposomes having a different lipid composition between their inner and outer membrane bilayers and able to reach primary tumors and their metastases after intravenous injection to animals and humans. The formulation method includes complex formation between DNA with cationic lipid molecules and fusogenic/NLS peptide conjugates composed of a hydrophobic chain of about 10-20 amino acids and also containing four or more histidine residues or NLS at their one end. The encapsulated molecules display therapeutic efficacy in eradicating a variety of solid human tumors including but not limited to breast carcinoma and prostate carcinoma. Combination of the plasmids, oligonucleotides or negatively-charged drugs with other anti-neoplastic drugs (the positively-charged cis-platin, doxorubicin) encapsulated into liposomes are of... |
| Insulin analogues of enhanced receptor-binding specificity | 20120184488 | 20120719 |
| A method of treating a patient includes administering a physiologically effective amount of an insulin analogue or a physiologically acceptable salt thereof to the patient. The insulin analogue or physiologically acceptable salt thereof contains an insulin A-chain sequence modified at positions selected from the group consisting of A0, A1, A4, A8, and A21. The insulin analogue may exhibit decreased affinity for the IGF receptor in comparison to wild type insulin of the same species and at least 20% of the affinity of wild-type insulin for the insulin receptor of the same species. Position A0 may be arginine. Position A1 may be D-alanine, D-aspartic acid, or D-leucine. Position A8 may be histidine, lysine, or arginine. Optionally, an insulin B-chain analogue sequence comprises a histidine at position B1.... |
| Lyaseenzymes, nucleic acids encoding them and methods for making and using them | 20120177722 | 20120712 |
| X═NO2, Cl, Br, NH2, OH, H, alkyl at one or several o, m, and p positions R═H or alkyl.
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| Method for fermentation culture in medium containing xylose | 20120149081 | 20120614 |
| The xylose-metabolizing ability and particularly the xylose incorporation rate, of yeast to which xylose-metabolizing ability has been imparted are significantly improved. The method according to the present invention comprises the steps of: culturing yeast having xylose-metabolizing ability in a xylose-containing medium in which the concentration of at least one amino acid selected from the group consisting of asparagine (Asn), serine (Ser), tyrosine (Tyr), threonine (Thr), and histidine (His) is increased; and recovering alcohol from the medium.
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| Protein purification | 20120149878 | 20120614 |
| Methods of reducing high molecular weight species (HMW) formation in a sample containing a protein purified using ion exchange (IEX) chromatography are disclosed, as are a number of related methods, e.g., methods of reducing on-column denaturation of a protein in a protein sample purified using an ion exchange (IEX) column or resin. The methods share characteristics of including arginine, glycine and/or histidine in the buffers used during the ion exchange (IEX) chromatography.
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| Aptamer that recognizes peptide | 20120129720 | 20120524 |
| An aptamer capable of binding to a histidine peptide is provided. A nucleic acid used as the aptamer capable of binding to a histidine peptide is any of the following nucleic acids (a) to (d): (a) a nucleic acid having a base sequence represented by SEQ ID NO: 17: GGUNnAYUmGGH (SEQ ID NO: 17), where in the nucleic acid (a), N represents A, G, C, U, or T, n of Nn represents the number of Ns and is an integer from 1 to 3, Y represents U, T, or C, m of Um represents the number of Us and is an integer from 1 to 3, and H represents U, T, C, or A; (b) a nucleic acid having a base sequence obtained by substitution, deletion,... |
| Compositions with antigens adsorbed to calcium phosphate | 20120121714 | 20120517 |
| Calcium phosphate is used as an adjuvant, with a high degree of antigen adsorption to the adjuvant. The invention is particularly useful for adjuvanting conjugated capsular saccharide antigens. Buffers, such as phosphate or histidine buffers, can advantageously be used in combination with the calcium phosphate, and compositions may have a pH in the range of 5.5 to 7.5.
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| Polypeptides having phytase activity and polynucleotides encoding same | 20120114799 | 20120510 |
| The invention relates to Citrobacter phytases derived from Citrobacter amalonaticus, Citrobacter gillenii, and related phytases. The phytases belong to the acid histidine phosphatase family, are acid-stable, and expectedly of a high specific activity. The invention also relates to the corresponding DNA, the recombinant and wild-type production of the phytases, as well as the use thereof, in particular in animal feed.
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| Pichia pastoris loci encoding enzymes in the histidine biosynthetic pathway | 20120100618 | 20120426 |
| Disclosed is the HIS7 gene encoding the His7p enzyme in the histidine biosynthesis pathway of Pichia pastoris. The locus in the Pichia pastoris genome encoding the His7p is useful sites for stable integration of heterologous nucleic acid molecules into the Pichia pastoris genome. The gene or gene fragment encoding the His7p may be useful as a selection marker for constructing recombinant Pichia pastoris.
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| Stabilization of immunoglobulins through aqueous formulation with histidine at weak acidic to neutral ph | 20120076772 | 20120329 |
| The present invention provides, among other aspects, storage stabile aqueous formulations of immunoglobulins with histidine at a mildly acidic to neutral pH. The present invention also provides methods for stabilizing immunoglobulin compositions by formulating with histidine at a mildly acidic to neutral pH. Advantageously, the methods and formulations provided herein allow stabile aqueous compositions of immunoglobulins at mildly acidic to neutral pH useful for parenteral administration.
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| Thioester-terminated water soluble polymers and method of modifying the n-terminus of a polypeptide therewith | 20120065330 | 20120315 |
| The invention provides reagents and methods for conjugating a polymer specifically to the α-amine of a polypeptide. The invention provides monofunctional, bifunctional, and multifunctional PEGs and related polymers having a terminal thioester moiety capable of specifically conjugating to the α-amine of a polypeptide having a cysteine or histidine residue at the N-terminus. The invention provides reactive thioester-terminated PEG polymers that have suitable reactivity with an N-terminal cysteine or histidine residue of a polypeptide to produce an amide bond between the PEG molecule and the polypeptide.
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| Methods for identifying fragile histidine triad (fhit) interaction and uses thereof | 20120010092 | 20120112 |
| Provided herein are methods and compositions for the diagnosis, prognosis and treatment of a cancer associated disorder using the Fhit gene.
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| Novel triple tag sequences and methods of use thereof | 20120010101 | 20120112 |
| The present disclosure relates to novel triple tag sequences that may comprise a 6× histidine tag, a c-myc tag and a V5 tag. The present disclosure also provides polynucleotides, proteins, vectors and host cells that comprise the triple tag sequence of the present disclosure, including libraries of such polynucleotides, proteins, vectors and host cells. The novel triple tag sequences of the present disclosure may be used in phage display vectors and phage libraries and in methods for detection, screening, capture, purification, quantitation, and/or recovery of proteins of interest to which they are linked. Proteins of interest include antibodies such as single chain antibodies, single chain antibodies, and Fab fragments of antibodies or peptides such as non-antibody peptides.
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| Histidine related compounds for identifying and blocking amyloid beta ion channels | 20110015139 | 20110120 |
| The present disclosure relates to amyloid beta (Aβ) channels and the diseases and disorders caused by abnormal activity in these channels, such as Alzheimer's disease, Lewy body dementia, inclusion body myositis, or cerebral amyloid angiopathy. The disclosure provides compositions and methods that block AO channel activity and/or reduce Aβ-induced toxicity in a cell. Compositions comprised of compounds having histidine coordinating capacity are used in methods to prevent, reduce, or eliminate damage caused by Aβ ion channels.
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| Poly zinc finger proteins with improved linkers | 20110014675 | 20110120 |
| Polynucleotides encoding chimeric proteins, and methods for their production and use are disclosed. The chimeric proteins comprise a flexible linker between two zinc finger DNA-binding domains, wherein the linker contains eight or more amino acids between the second conserved histidine residue of the carboxy-terminal zinc finger of the first domain and the first conserved cysteine residue of the amino-terminal zinc finger of the second domain.
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| Methods and compositions for increasing the anaerobic working capacity in tissues | 20110009346 | 20110113 |
| Provided are compositions comprising beta-alanylhistidine peptides and/or beta-alanines, and methods for administering these peptides and amino acids. In one aspect, the compositions and methods cause an increase in the blood plasma concentrations of beta-alanine and/or creatine.
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| Multi block copolymers | 20110003970 | 20110106 |
| A multi-block copolymer comprises at least one hydrophilic collagen-like block and at least one silk-like block. The silk-like block comprises an amino acid sequence ((GA)mGX)n (SEQ ID NO: 10), wherein G is glycine, A is alanine, m and n are at least 2. X is an ionizable amino acid. The ionizable amino acid can be inducedle to bear a positive charge or a negative charge. The ionizable amino acid bearing the positive charge is preferably histidine and the one bearing the negative charge is preferably glutamic acid.
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| Methods for increasing the therapeutic efficacy of immunoglobulin g class 3 (igg3) antibodies | 20110003336 | 20110106 |
| The present invention relates to methods for increasing the therapeutic efficacy of immunoglobulin G class 3 (IgG3) antibodies, immunoglobulin G class 3 (IgG3) antibodies with an improved therapeutic efficacy and the use thereof as a medicament, in particularly a medicament for immunotherapy. Specifically, the present invention relates to methods for increasing the therapeutic efficacy of an immunoglobulin G class 3 (IgG3) antibody comprising providing a mutated immunoglobulin G class 3 (IgG3) antibody, wherein the mutation, as compared to the parent immunoglobulin G class 3 (IgG3) antibody, comprises a replacement of the amino acid arginine (R) at position 435 in the CH3 domain with the amino acid histidine (H), and antibodies obtained by the present methods and their use as a medicament.
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| Processes of making and using pharmaceutical formulations of antineoplastic agents | 20100331382 | 20101230 |
| In its several embodiments, this invention discloses a pharmaceutical formulation comprising at least one antineoplastic agent or a pharmaceutically acceptable salt thereof, and at least one dissolution enhancing agent sufficient to substantially dissolve said at least one antineoplastic agent in at least one aqueous diluent, wherein said dissolution enhancing agent is urea, L-histidine, L-threonine, L-asparagine, L-serine, L-glutamine or mixtures thereof; a lyophilized powder comprising said pharmaceutical formulation, and articles of manufacture thereof.
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| Histidine and/or histidine derivative for the treatment of inflammatory skin diseases | 20100331235 | 20101230 |
| Histidine and/or a derivative thereof. In some embodiments, the histidine and/or a derivative thereof is used in maintaining and/or improving barrier function of the skin of a subject. In some embodiments, the histidine and/or a derivative thereof is used for the prevention and/or treatment of an inflammatory skin disease.
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| Therapeutic agent for cerebral ischemic injury | 20100323975 | 20101223 |
| A therapeutic agent for cerebral ischemic injury contains at least one selected from L-alanyl-L-histidine and glycyl-L-histidine as an active ingredient. The therapeutic agent for cerebral ischemic injury preferably has a dosage form as an injection for intravenous administration. The therapeutic agent for cerebral ischemic injury having a dosage form as an aqueous injection contains at least one selected from L-alanyl-L-histidine and glycyl-L-histidine at a concentration of preferably 0.3 to 3.5 mol/L, and more preferably 0.6 to 2.1 mol/L.
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| Probe compounds for protein tyrosine phosphatase (ptp) and precursors thereof | 20100317831 | 20101216 |
| In Formula (I), A1 and A2 represent amino acids. The amino acids include leucine, phenylalanine, glutamic acid, lysine, alanine, arginine, aspartic acid, asparagine, citrulline, cysteine, cystine, glutamine, glycine, histidine, hydroxyproline, isoleucine, methionine, proline, serine, threonine, tryptophan, valine or a combination thereof. The invention also provides probe compound precursors for protein tyrosine phosphatases (PTPs).
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| Stabilized factor ix formulations containing trehalose | 20100316625 | 20101216 |
| Methods of preparing lyophilized preparations of Factor IX which preserve more than 90% of the calcium binding property of Factor IX are disclosed. Factor IX formulated with trehalose shows a superior stability profile after 12 weeks storage at 25° C./60% relative humidity (RH) and 40° C./75% RH relative to Factor IX formulated without trehalose. The data suggest that the inclusion of trehalose in the formulation could allow for temperature excursions or even long-term room temperature storage of a Factor IX lyophilized product. The formulations tested contained 10 mM histidine pH 6.8, 3% mannitol, 66 mM sodium chloride, 0.0075% Polysorbate 80, with and without 1% trehalose. Upon storage at 40° C./75% RH or 25° C./60% RH over 12 weeks the trehalose-containing formulation was comparable to product stored... |
| Aqueous preparation comprising emip as active ingredient | 20100316592 | 20101216 |
| An objective of the present invention is to provide aqueous preparations comprising eMIP, a derivative of macrophage inflammatory protein 1α (MIP-1α) which has an immunopotentiation activity, and stabilizer(s). The present inventors conducted dedicated studies to achieve the above-described objective. As a result, the present inventors discovered that eMIP degradation is suppressed by addition of at least one or more additives selected from sodium chloride, L-histidine, L-arginine, L-arginine hydrochloride, L-lysine hydrochloride, citric acid, and sodium edetate (EDTA). Furthermore, the present inventors demonstrated that phosphate buffer of pH 5 to pH 7 is a preferable pH adjuster for the aqueous eMIP preparations of the present invention.
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| Novel compounds, use thereof in cosmetic and cosmeceutic applications, and compositions comprising same | 20100311667 | 20101209 |
| A compound of the formula I: R-A-Gly-His-B (I) wherein: A and B are independently of each other a L-lysine residue, a D-lysine residue, or a L- or D-lysine residue in which the NH2 group of the side chain comprises a modification, where-in said modification is (i) a replacement with a hydrogen, (ii) an acetylation, (iii) a benzoylation, or (iv) a palmitoylation; GIy is a glycine residue; His is a L- or D-histidine residue; R is CH3—(CH2)n—CO—, wherein n=2, 3, 4, 5, 6, 7 or 8; R′ is a group of formula (II): N(Z)(Z′) (II) wherein: Z and Z′ is hydrogen, a methyl group, an ethyl group, a phenyl group, an hexyl group, a decyl group or an hexadecyl group; or a racemate, an enantiomer or a... |
| Novel peptides, use thereof in cosmetic and cosmeceutic applications, and compositions comprising same | 20100310484 | 20101209 |
| A peptide of formula I (SEQ ID NO: 1): Lip-A-Gly-His-B-R (I) wherein: Lip is a lipoyl residue of R or S configuration; A is absent or is a lysine residue of configuration L or D; GIy is a glycine residue; His is a histidine residue of configuration L or D; B is a lysine residue of configuration L or D, or a lysine residue of configuration L or D in which the NH2 group of the side chain comprises a modification, wherein said modification is (i) a replacement with a hydrogen or (ii) a modification with a protecting group selected from the group consisting of acetyl, benzoyl, tosyl, sulfonyl benzene, benzyloxycarbonyle and palmitoyl; wherein R is O(Z) or N(Z′)(Z′), and wherein Z, Z′ and Z′ are... |
| Anti-il-9 antibody formulations and uses thereof | 20100303736 | 20101202 |
| The present invention provides liquid formulations of antibodies or antibody fragments that immunospecifically bind to an IL-9 polypeptide, which formulations exhibit stability, low to undetectable levels of aggregation, and very little to no loss of the biological activities of the antibodies or antibody fragments, even during long periods of storage. In particular, the present invention provides liquid formulations of antibodies or fragments thereof that immunospecifically bind to an IL-9 polypeptide, which formulations are substantially free of surfactants, sugars, sugar alcohols, amino acids other than histidine (preferably with pKa values of less than 5 and above 7), and/or other common excipients. Furthermore, the invention provides methods of preventing, treating or ameliorating a disease or disorder associated with or characterized by aberrant expression and/or activity of an IL-9... |
| Thermal treatment process for tobacco materials | 20100300463 | 20101202 |
| A method of thermally processing a tobacco material is provided, the method including the steps of (i) mixing a tobacco material, water, and an additive selected from the group consisting of lysine, glycine, histidine, alanine, methionine, glutamic acid, aspartic acid, proline, phenylalanine, valine, arginine, di- and trivalent cations, asparaginase, saccharides, phenolic compounds, reducing agents, compounds having a free thiol group, oxidizing agents, oxidation catalysts, plant extracts, and combinations thereof, to form a moist tobacco mixture; (ii) heating the moist tobacco mixture at a temperature of at least about 60° C. to form a heat-treated tobacco mixture; and (iii) incorporating the heat-treated tobacco mixture into a tobacco product. Heat-treated tobacco composition prepared according to the method are also provided, such as heat-treated smokeless tobacco composition comprising a... |
| Fusion tag comprising an affinity tag and an ef-hand motif containing polypeptide and methods of use thereof | 20100297734 | 20101125 |
| The application discloses a fusion tag comprising an affinity tag and a polypeptide comprising one or more EF hand motif(s). Preferably, said fusion tag comprises a polyhistidine tag, one or more EF hand motif(s) of calmodulin and a thrombin cleavage site. Methods of using said fusion tag to purify a polypeptide of interest are also disclosed.
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| Transformed cell with enhanced sensitivity to antifungal compound and use thereof | 20100291607 | 20101118 |
| The present invention provides a transformed cell in which a polynucleotide having a nucleotide sequence encoding an amino acid sequence of an osmosensing histidine kinase having no transmembrane region is introduced in a functional form into a cell deficient in at least one hybrid-sensor kinase, a method of assaying the antifungal activity of a test substance using the transformed cell, and a method of searching an antifungal compound using the method, and the like.
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| Polypeptides having phytase activity and polynucleotides encoding same | 20100287634 | 20101111 |
| The invention relates to Citrobacter phytases derived from Citrobacter amalonaticus, Citrobacter gillenii, and related phytases. The phytases belong to the acid histidine phosphatase family, are acid-stable, and expectedly of a high specific activity. The invention also relates to the corresponding DNA, the recombinant and wild-type production of the phytases, as well as the use thereof, in particular in animal feed.
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| Cationic peptide for delivering an agent into a cell | 20100286069 | 20101111 |
| There is presently provided a triblock peptide comprising a hydrophobic amino acid block, a histidine block and a cationic amino acid block. The triblock peptide may be used to form a nanoparticle for delivery of an agent into a cell.
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| Transformed cell with enhanced sensitivity to antifungal compound and use thereof | 20100285511 | 20101111 |
| The present invention provides a transformed cell in which a polynucleotide having a nucleotide sequence encoding an amino acid sequence of an osmosensing histidine kinase having no transmembrane region is introduced in a functional form into a cell deficient in at least one hybrid-sensor kinase, a method of assaying the antifungal activity of a test substance using the transformed cell, and a method of searching an antifungal compound using the method, and the like.
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| Use of a gene encoding a histidine protein kinase to create drought resistant plants | 20100281580 | 20101104 |
| Plant expression vectors that include promoter sequences operably linked to heterologous ATHK1 polynucleotides, or complements thereof, encoding polypeptides at least 95% identical to SEQ ID NO:26, where the polynucleotides encode polypeptides that confers drought resistance in the plants. Also provided are transgenic plants with increased drought resistance, methods for creating such plants, overexpressors, and underexpressors of ATHK1. Methods for enhancing drought resistance in plants are also provided.
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| Detection of plasmodium falciparum histidine-rich protein ii in saliva malaria patients | 20100279319 | 20101104 |
| The detection of PfHRP II in saliva offers a practical, cost-effective alternative to PfHRP II detection in blood as a means for diagnosis of malaria. Collection of saliva is non-invasive, simple, safe, stress free, painless and can be accomplished in primitive settings. The use of Malaria Antigen ELISA kits (CELISA, Cellabs, Australia) used in accord with known procedures for testing blood samples.
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| System and method for identifying complex patterns of amino acids | 20100278860 | 20101104 |
| A method and system are disclosed for identifying and/or locating complex patterns in an amino acid sequence stored in a computer file or database. According to an aspect of the present invention, techniques are provided to facilitate queries of protein databases. For protein descriptions received in response to the queries, embodiments of the present invention may scan the received protein descriptions to identify and locate Replikin patterns. A Replikin pattern is defined to be a sequence of 7 to about 50 amino acids that include the following three (3) characteristics, each of which may be recognized by an embodiment of the present invention: (1) the sequence has at least one lysine residue located six to ten amino acid residues from a second lysine residue; (2) the... |
| Methods and kits for predicting treatment response in type ii diabetes mellitus patients | 20100273661 | 20101028 |
| A method for predicting treatment response of a type II diabetes patient to rosiglitazone is provided. The method involves at least one sample from a patient having type II diabetes and analyzing biomarkers predictive of a patient who will respond to treatment with rosiglitazone. The biomarkers include, at least, interleukin-8, histidine, citrate. These biomarkers are identified in at least one classification analyses selected from the group consisting of a majority-vote based classifier and support-vector machine (SVM) classifier. Also provided is a method for predicting treatment response of a type II diabetes patient to glyburide at 8 weeks post-initiation of therapy. The method involves obtaining a sample from a type II diabetes patient who has been treated with glyburide for about 4 weeks and analyzing biomarkers predictive... |
| Anti-fatigue agent comprising amino acid composition | 20100267794 | 20101021 |
| Conventional amino acid compositions are primarily intended to improve athletic performance or to promote fat-burning. Provided is an anti-fatigue agent which can prevent both of muscle fatigue and nerve strain concurrently. An anti-fatigue agent which comprises an amino acid composition composed of specific amino acids in specified amounts can prevent both of muscle fatigue and nerve strain concurrently. As for the types and the ratio of the amounts of the amino acids contained in the amino acid composition, the amino acid composition preferably contains 30 to 200 parts by weight of proline, 60 to 140 parts by weight of glycine, 50 to 260 parts by weight of alanine, 50 to 130 parts by weight of lysine, 30 to 75 parts by weight of tryptophan and 20... |
| Dipeptides as feed additives | 20100247707 | 20100930 |
| The invention relates to feed additives containing dipeptides or salts thereof, in which one amino acid residue of the dipeptide is a DL-methionyl residue and the other amino acid residue of the dipeptide is an amino acid in the L-configuration selected from lysine, threonine, tryptophan, histidine, valine, leucine, isoleucine, phenylalanine, arginine, cysteine and cystine; feed mixtures containing these additives and method of producing the dipeptides.
... |
| Copper-zinc alloy electroplating bath and plating method using the copper-zinc alloy electroplating bath | 20100243466 | 20100930 |
| The copper-zinc alloy electroplating bath comprises at least one selected from a copper salt, zinc salt, alkali metal pyrophosphate, and amino acid or a salt thereof, and has a pH of 8.5 to 14. The pH is preferably 10.5 to 11.8; and the concentration of the amino acid or a salt thereof is preferably 0.08 mol/L to 0.22 mol/L, more preferably 0.1 mol/L to 0.13 mol/L. As the amino acid or a salt thereof, histidine or a salt thereof may be preferably used.
... |
| Replikins and methods of identifying replikin-containing sequences | 20100240876 | 20100923 |
| The present invention provides methods for identifying a class of peptides referred to as replikins and methods of using replikins to stimulate the immune system of a subject. The method of identifying replikin peptides is based on identifying amino acid sequences comprising 7 to about 50 amino acids that contain (1) at least one lysine residue located six to ten residues from a second lysine residue; (2) at least one histidine residue; and (3) at least 6% lysine residues.
... |
| Antioxidant constituents | 20100240599 | 20100923 |
| An object of the present invention is to provide an antioxidant composition that is effective in the living body against active oxygen species produced in the body. The present invention provides an antioxidant composition having the effect of suppressing three active oxygen species, i.e. hypochlorite radicals, hydroxyl radicals, and peroxynitrite radicals, with respect to active oxygen species produced in the body, the antioxidant composition comprising a mixture in which at least 20 mg of vitamin C (L-ascorbic acid or sodium L-ascorbate) as an agent to scavenge peroxynitrite active oxygen, and at least 2 mg of caffeic acid analogue compound(s), at least 10 mg of polyphenyol compound(s) or at least 1.5 mg of carotenoid compound(s) as an agent to scavenge hydroxyl radical active oxygen are combined with... |
| Novel conjugated proteins and peptides | 20100239517 | 20100923 |
| The invention provides a novel process for conjugating a polymer, especially PEG, to a protein or peptide, which comprises reacting a polymeric conjugation reagent with a protein or peptide containing a polyhistidine tag under conditions such that conjugation occurs via said polyhistidine tag. The resulting conjugates are novel. The invention further relates to novel conjugates of the general formula (I) in which one of X and X′ represents a polymer, and the other represents a hydrogen atom; each Q independently represents a linking group; W represents an electron-withdrawing moiety or a moiety preparable by reduction of an electron-withdrawing moiety; or, if X′ represents a polymer, X-Q-W— together may represent an electron withdrawing group; and in addition, if X represents a polymer, X′ and electron withdrawing group... |
| Superparamagnetic nanoparticles based on iron oxides with modified surface, method of their preparation and application | 20090309597 | 20091217 |
| The preparation of labelled cells proceeds by adding to the complete culture medium 5-20 μl, to advantage 10 μl, of a colloid containing 0.05-45 mg iron oxide per ml, to advantage 1-5 mg iron oxide per ml of the medium, and culturing the cells for a period of 1-7 days, to advantage for 1-3 days, at 37° C. and 5% of CO2.
... |
| Prophylactic or therapeutic composition for hemoglobinuria or myoglobinuria | 20090306208 | 20091210 |
| According to the present invention, the prophylactic or therapeutic composition for hemoglobinuria or myoglobinuria which comprises a branched-chain amino acid such as valine, leucine or isoleucine or a salt thereof, a basic amino acid such as ornithine, arginine, lysine, histidine or citrulline or a salt thereof and glutamine or a salt thereof as active ingredients can be provided.
... |
| Dipeptide compounds containing d-histidine | 20090306165 | 20091210 |
| D-Camosine lipophilic derivatives are disclosed, characterized by higher bioavailability than L-camosine and intended for the pulmonary distribution where they can exert detoxifying activity on the cytotoxic carbonyl compounds induced by cigarette smoke.
... |
| Stabilized parathyroid hormone composition comprising parathyroid hormone, buffer and stabilizing agent | 20090305965 | 20091210 |
| Disclosed relates to a stabilized parathyroid hormone (PTH) comprising a buffer and a stabilizing agent and, more particularly, to a stabilized PTH composition in which succinic acid, malic acid, histidine or ammonium bicarbonate is used as the buffer and sorbitol or mannitol is used as the stabilizing agent. The PTH composition of the present invention can be used to formulate stably PTH protein that is much more unstable to be readily decomposed than normal low molecular weight drugs.
... |
| Histidine-containing diastereomeric peptides and uses thereof | 20090305954 | 20091210 |
| Diastereomeric peptides with a net positive charge greater than +1, and cyclic derivatives thereof, are provided, having at least 13 amino acid residues, comprising histidine and one or more hydrophobic amino acid residues, optionally esterified or amidated at the C-terminus and/or acylated at the N-terminus. The peptides may contain other amino acid residues including non-natural amino acids. The peptides are particularly useful in the treatment of cancer.
... |
| Fibrillation resistant proteins | 20090304814 | 20091210 |
| Protection of proteins against fibrillation may be afforded by introduction of certain histidine substitutions into the protein, such that a pair of histidines are present with sufficient spacing as to allow the histidines to coordinate with zinc. In the case of insulin, introduction of histidine residue substitutions at residues A4 and A8 together or a histidine residue substitution at residue B1, provides increased resistance to fibrillation while maintaining at least a majority of the activity of the insulin analogue. Introduction of a histidine residue substitution at residue A8 restores at least a portion of fibrillation resistance that may have been harmed by substitutions present on the B-chain such as those present in fast-acting insulins. Proteins protected by such histidine substitutions may be used to provide a... |
| Stabilized antibody-containing formulations | 20090291076 | 20091126 |
| The present invention relates to antibody-containing lyophilized formulations free from reducing sugars, non-reducing sugars, sugar alcohols or polysaccharides as excipients and including one or more amino acid selected from the group consisting of arginine, histidine, lysine, serine, proline, glycine, alanine and threonine or a salt thereof.
... |
| Method of production of recombinant sucrose synthase, use thereof in the manufacture of kits for determination of sucrose, production of adpglucose and production of transgenic plants whose leaves and storage organs accumulate high contents of adpglucose | 20090288219 | 20091119 |
| A method is described for efficient production of large quantities of soluble recombinant SS in its active form, by expression of the gene that encodes SS in a strain of Escherichia coli. The expression vector used means that the recombinant SS produced possesses a histidine tail which facilitates its quick purification. In addition it describes sequences of mutated versions of the gene of SS that encode isoforms of SS suitable for the production of ADPG. Making use of the “wild-type” and “mutated” versions of recombinant SS, an efficient method is described for production of ADPG and UDPG. It also describes the use of SS for the production of assay kits for the determination of sucrose. Finally, it describes the production of transgenic plants which overexpress the... |
| Method of enhancing electrotransport polypeptide flux by amino acid substitution with histidine | 20090275877 | 20091105 |
| Methods of modifying polypeptide drugs in order to enhance their transdermal electrotransport flux are provided. The polypeptide is modified by substituting a histidine residue (His) for one or more glutamine (Gln), threonine (Thr) and/or asparagine (Asn) residue(s). The His for Gln substitution is particularly preferred from the standpoint of retaining biological activity of the parent polypeptide. Compositions containing the modified polypeptide, which are useful for transdermal electrotransport delivery, are also provided.
... |
| Mutant phosphoribosylpyrophosphate synthetase and method for producing l-histidine | 20090275089 | 20091105 |
| The present invention relates to a mutant bacterial PRPP synthetase which is resistant to feedback by purine nucleotides, and a method for producing L-histidine using the bacterium of the Enterobacteriaceae family wherein the L-amino acid productivity of said bacterium is enhanced by use of the PRPP synthetase which is resistant to feedback by purine nucleotides, coded by the mutant prsA gene.
... |
| Ph-sensitive polymeric micelles for drug delivery | 20090274753 | 20091105 |
| Mixed micelles containing poly(L-histidine)-poly(ethylene glycol) block copolymer and poly(L-lactic acid)-poly(ethylene glycol) block copolymer are a pH-sensitive drug carrier that release the drug in an acidic microenvironment, but not in the blood. Since the microenvironment of solid tumors is acidic, these mixed micelles are useful for treating cancer, including those cancers exhibiting multidrug resistance. Targeting ligands, such as folate, can also be attached to the mixed micelles for enhancing drug delivery into cells. Methods of treating a warm-blooded animal with such a drug are disclosed.
... |
| Method of enhancing electrotransport polypeptide flux by amino acid substitution with histidine | 20090275877 | 20091105 |
| Methods of modifying polypeptide drugs in order to enhance their transdermal electrotransport flux are provided. The polypeptide is modified by substituting a histidine residue (His) for one or more glutamine (Gln), threonine (Thr) and/or asparagine (Asn) residue(s). The His for Gln substitution is particularly preferred from the standpoint of retaining biological activity of the parent polypeptide. Compositions containing the modified polypeptide, which are useful for transdermal electrotransport delivery, are also provided.
... |
| Mutant phosphoribosylpyrophosphate synthetase and method for producing l-histidine | 20090275089 | 20091105 |
| The present invention relates to a mutant bacterial PRPP synthetase which is resistant to feedback by purine nucleotides, and a method for producing L-histidine using the bacterium of the Enterobacteriaceae family wherein the L-amino acid productivity of said bacterium is enhanced by use of the PRPP synthetase which is resistant to feedback by purine nucleotides, coded by the mutant prsA gene.
... |
| Ph-sensitive polymeric micelles for drug delivery | 20090274753 | 20091105 |
| Mixed micelles containing poly(L-histidine)-poly(ethylene glycol) block copolymer and poly(L-lactic acid)-poly(ethylene glycol) block copolymer are a pH-sensitive drug carrier that release the drug in an acidic microenvironment, but not in the blood. Since the microenvironment of solid tumors is acidic, these mixed micelles are useful for treating cancer, including those cancers exhibiting multidrug resistance. Targeting ligands, such as folate, can also be attached to the mixed micelles for enhancing drug delivery into cells. Methods of treating a warm-blooded animal with such a drug are disclosed.
... |
| Multifunctional biomaterials as scaffolds for electronic, optical, magnetic, semiconducting, and biotechnological applications | 20090269619 | 20091029 |
| One-dimensional ring structures from M13 viruses were constructed by two genetic modifications encoding binding peptides and synthesis of a heterobifunctional linker molecule. The bifunctional viruses displayed an anti-streptavidin peptide and hexahistidine (SEQ ID NO:4) peptide at opposite ends of the virus as pIII and pIX fusions. Stoichiometric addition of the streptavidin-NiNTA linker molecule led to the reversible formation of virus-based nanorings with circumferences corresponding to lengths of the packageable DNAs. These virus-based ring structures can be further engineered to nucleate inorganic materials and form metallic, magnetic, or semiconductor nanorings using trifunctionalized viruses.
... |
| Multifunctional biomaterials as scaffolds for electronic, optical, magnetic, semiconducting, and biotechnological applications | 20090269619 | 20091029 |
| One-dimensional ring structures from M13 viruses were constructed by two genetic modifications encoding binding peptides and synthesis of a heterobifunctional linker molecule. The bifunctional viruses displayed an anti-streptavidin peptide and hexahistidine (SEQ ID NO:4) peptide at opposite ends of the virus as pIII and pIX fusions. Stoichiometric addition of the streptavidin-NiNTA linker molecule led to the reversible formation of virus-based nanorings with circumferences corresponding to lengths of the packageable DNAs. These virus-based ring structures can be further engineered to nucleate inorganic materials and form metallic, magnetic, or semiconductor nanorings using trifunctionalized viruses.
... |
| Intraocular irrigating solutions and methods for treating corneal edema | 20090264375 | 20091022 |
| One aspect of the present invention relates to methods of treating corneal edema comprising contacting a cornea with an ophthalmic irrigating composition comprising histidine. In certain embodiments, the ophthalmic irrigating compositions contact the corneal endothelium. Another aspect of the present invention relates to ophthalmic irrigating compositions for treating corneal edema comprising histidine and optionally, calcium glycerophosphate and/or glutathione disulfide.
... |
| Skin cosmetic | 20090258964 | 20091015 |
| The present invention provides a skin cosmetic having superior sensation during use and stability and also maximally manifesting the various effects of ingredient (A), which is β-alanyl-L-histidine and/or its salt, by preparing a mildly acidic skin cosmetic by characteristically using ingredient (A) and ingredient (B), which is a thickener composed of a specific microgel chosen from many cosmetic thickeners, and adding ingredient (C), which is an inorganic acid and/or organic acid.
... |
| Method for production of a bioengineered form of tissue plasminogen activator | 20090246188 | 20091001 |
| The present invention relates to the recombinant method used for the production of soluble form of human tissue plasminogen activator variant. In this variant the threonine at position 103 of the endogenous tissue plasminogen activator is replaced by an asparagine leading to a new glycosylation site. At position 117 of the endogenous tissue plasminogen activator asparagine has been replaced by glutamine, leading to the removal of an N linked glycosylation site. At position 296-299 the amino acids lysine, histidine, arginine, and arginine have been replaced by four alanine amino acids. The invention further relates to the de novo synthesis of the nucleic acid sequence encoding tissue plasminogen activator, transformation of the constructed nucleic acid sequences into competent bacteria and sub-cloning of the same into mammalian expression... |
| Peptide derivatives with therapeutic activity | 20090247601 | 20091001 |
| Dipeptide compounds containing a histidine residue proved to have interesting blocking activity on secondary products from lipid oxidative stress, in particular on unsaturated aldehydes such as malondialdehyde and hydroxynonenal, which are known to contribute to the inset of quite a number of chronic pathologies such as neurodegenerative, inflammatory chronic, cardiovascular diseases, diabetes complications and cataract.
... |
| Mutant strains of lactic acid bacteria having a non-phosphorylable lactose permease | 20090238921 | 20090924 |
| The invention concerns lactic acid bacteria strains wherein the phosphorylable histidine of the IIA domain of lactose permease is replaced by a non-phosphorylable amino acid. Said strains have a reduced post-acidification and are useful in particular for preparing fermented dairy products.
... |
| Rumen protected essential amino acids | 20090232960 | 20090917 |
| Use of essential amino acid imines and compositions containing them as a source of rumen protected essential amino acids for ruminant animals. Preferred are histidine and methionine.
... |
| Composition for introduction of nucleic acid | 20090233366 | 20090917 |
| wherein (R1)n represents a polyamino acid residue consisting of a total of n amino acid residues, which are identical to or different from one another, the n residues being selected from an arginine residue, a lysine residue, and a histidine residue, and n being an integer of from 4 to 16; R2 represents a single bond or an amino acid residue; and R3 represents a phospholipid residue with 1 or 2 identical or different unsaturated fatty acid residues having from 12 to 20 carbon atoms. The composition is administered or supplied to a cell together with a nucleic acid.
... |
| Cytokinin-sensing histidine kinases and methods of use | 20090235392 | 20090917 |
| Isolated polynucleotides that encode cytokinin-sensing histidine kinase polypeptides, and the encoded polypeptides, are described. Expression cassettes comprising the polynucleotides of the invention and plants and plant cells that are transformed with the polynucleotides are described. Methods of using the cytokinin-sensing histidine kinase polypeptides and polynucleotides to modulate histidine kinase activity and/or histidine kinase levels in plants and plant cells are further described.
... |
| Rumen protected essential amino acids | 20090232960 | 20090917 |
| Use of essential amino acid imines and compositions containing them as a source of rumen protected essential amino acids for ruminant animals. Preferred are histidine and methionine.
... |
| Composition for introduction of nucleic acid | 20090233366 | 20090917 |
| wherein (R1)n represents a polyamino acid residue consisting of a total of n amino acid residues, which are identical to or different from one another, the n residues being selected from an arginine residue, a lysine residue, and a histidine residue, and n being an integer of from 4 to 16; R2 represents a single bond or an amino acid residue; and R3 represents a phospholipid residue with 1 or 2 identical or different unsaturated fatty acid residues having from 12 to 20 carbon atoms. The composition is administered or supplied to a cell together with a nucleic acid.
... |
| Cytokinin-sensing histidine kinases and methods of use | 20090235392 | 20090917 |
| Isolated polynucleotides that encode cytokinin-sensing histidine kinase polypeptides, and the encoded polypeptides, are described. Expression cassettes comprising the polynucleotides of the invention and plants and plant cells that are transformed with the polynucleotides are described. Methods of using the cytokinin-sensing histidine kinase polypeptides and polynucleotides to modulate histidine kinase activity and/or histidine kinase levels in plants and plant cells are further described.
... |
| Method of producing recombinant tat-hoxb4h protein for use as a stimulant of hematopoiesis in vivo | 20090227496 | 20090910 |
| The present invention relates to a new and nonobvious method of producing the C-terminal histidine tagged TAT-HOXB4 fusion protein (TAT-HOXB4H), providing unexpected benefits of increased yield and stability to allow for in vivo administration of this protein, and pharmaceutical composition comprising an effective ingredient, TAT-HOXB4H, having stimulatory activity on the production of hematopoietic cells. More specifically, recombinant TAT-HOXB4H protein enhances engraftment of bone marrow transplants, hematopoietic reconstruction, bone marrow re-population and number of circulating stem cells, particularly after chemotherapy or irradiation.
... |
| Antibodies active against a fusion polypeptide comprising a histidine portion | 20090221040 | 20090903 |
| The present invention relates to an antibody active against a fusion polypeptide comprising a histidine portion, a process for the preparation thereof and its use.
... |
| Peptide amidation process | 20090215987 | 20090827 |
| The invention provides a process for amidating a desired peptide comprising cleaving a substrate polypeptide at a X1-cysteine sequence, wherein X1 is the amino acid at the peptide carboxyl-terminus and cysteine is the first amino acid of a palladium cleavage site comprising the sequence cysteine-X2-X3, wherein X2 is any amino acid, X3 is an amino acid selected from the group consisting of cysteine, histidine, or methionine, and wherein the carboxyl-terminus of the peptide is amidated upon cleavage at the X1-cysteine sequence.
... |
| Polypeptides having phytase activity and polynucleotides encoding same | 20080292753 | 20081127 |
| The invention relates to a phytase derived from Citrobacter braakii and related phytases. The phytases belong to the acid histidine phosphatase family, are acid-stable, of an excellent performance in animal feed, of a high specificity towards the substrate phytate, and expectedly of a high specific activity. The invention also relates to the corresponding DNA, the recombinant and wild-type production of the phytases, as well as the use thereof.
... |
| Diagnosis of neurodegenerative diseases | 20080286263 | 20081120 |
| The invention relates to a method of diagnosis of Huntington's Disease in a diagnostic sample of a valid body tissue taken from a human subject, which comprises detecting an altered concentration of a protein in the diagnostic sample, compared with a sample of a control human subject, the protein being selected from: Swiss Prot accession number: Protein name; P10909: Clusterin precursor; P00738: Haptoglobin precursor; P01009: Alpha-1-antitrypsin precursor; P01024: Complement C3 precursor; P01620: 1 g kappa chain V-III region; P01834: 1 g kappa chain C region P01842: 1 g lambda chain C regions; P01857: 1 g gamma-1 chain C region; P01859: Ig gamma-2 chain C region; P01876: 1 g alpha-1 chain C region P02647: Apolipoprotein A-I precursor; P02649: Apolipoprotein E precursor; P02652: Apolipoprotein A-II precursor; P02655: Apolipoprotein... |
| Replikins and mentods of identifying replikin-containing sequences | 20080275214 | 20081106 |
| The present invention provides methods for identifying a class of peptides referred to as replikins and methods of using replikins to stimulate the immune system of a subject. The method of identifying replikin peptides is based on identifying amino acid sequences comprising 7 to about 50 amino acids that contain (1) at least one lysine residue located six to ten residues from a second lysine residue; (2) at least one histidine residue; and (3) at least 6% lysine residues.
... |
| Compositions and approaches for increasing diet induced thermogenesis, inducing weight loss and maintaining muscle mass and strength | 20080268038 | 20081030 |
| Provided are compositions and methods for increasing diet induced thermogenesis. Typically, the compositions are comprised of L-histidine, L-isoleucine, L-leucine, L-lysine, L-methionine, L-phenylalanine, L-valine and L-threonine.
... |
| Universal procoagulant | 20080260858 | 20081023 |
| A thromboplastin reagent comprises: (i) activated sTF, (ii) a metal-chelating lipid, (iii) a metal ion, and (iv) a phospholipid. Activated sTF preferably includes the extracellular domain of TF and an oligohistidine moiety having at least 2 histidine residues, more preferably 2-10 histidine residues. Preferably, the histidine residues are consecutive. Attaching a metal binding domain, such as an oligohistidine tag, to the C-terminus of sTF allows the protein to bind to phospholipid vesicles that contain metal-chelating lipid. Metal complexes of this activated sTF and metal-chelating lipids have all of the desirable expression, handling, and solubility characteristics of sTF, and exhibit procoagulant activities in plasma clotting tests that are comparable to relipidated rTF. In addition, it was discovered that, under some circumstances, Ni-lipids are themselves procoagulant, even in... |
| Rumen protected essential amino acids | 20080255219 | 20081016 |
| Use of essential amino acid imines and compositions containing them as a source of rumen protected essential amino acids for ruminant animals. Preferred are histidine and methionine.
... |
| Pharmaceutical preparation for the treatment of shock | 20080249006 | 20081009 |
| which peptide has the biological property of matching the inducible VE-cadherin binding motif on the Bβ-chain (i.e. Bβ15-42) of human fibrin, for the preparation of a pharmaceutical preparation for the treatment of shock.
... |
| Analysis apparatus and analysis method for glycosylated hemoglobin | 20080223733 | 20080918 |
| Disclosed is a method for calculating a ratio of glycosylated hemoglobin with high accuracy by electrochemically detecting the concentration of fructosyl valine or fructosyl valyl-histidine in a sample. Also disclosed is an apparatus for assaying glucose and glycosylated hemoglobin simultaneously. Further disclosed are a method and an apparatus for removing hydrogen peroxide in a sample.
... |
| Personal care composition | 20080206169 | 20080828 |
| Personal care composition comprising at least one skin care active selected from the group consisting of acetyl glutamic acid, acetyl glutamine, acetyl methionine, acetyl tributyl citrate, acetyl triethyl citrate, acetyl tyrosine, adipic acid, alanine, arginine, arginine glutamate, benzophenone-3, camphor, gluconolactone, glucose, glycine, histidine hydrochloride, hydroxyproline, maltitol, phenylalanine, succinic acid, buffered lactic acid, tris(tetramethylhydroxypiperidinol) citrate, a boswellic acid compound, and salts, isomers, derivatives, and mixtures of any of the foregoing; and a dermatologically acceptable carrier.
... |
| Treatment of copd, gastro-esophageal reflux disease (gerd), food allergies and other gastrointestinal conditions and disorders ameliorated by proper histamine management using a combination of histidine decarboxylase inhibitors, lra drugs, anti-h1 and/or | 20080207530 | 20080828 |
| The invention provides a method for the treatment of COPD and/or gastrointestinal disease conditions ameliorated by histamine management in a subject, comprising administering to the subject an effective amount of a histidine decarboxylase inhibitor.
... |
| Sensitization of immune system against haptenized melanoma antigens | 20080199425 | 20080821 |
| The invention is based on the observation that certain phenols, monophenols or benzenediols, can be metabolized into reactive quinones, in particular ortho-quinones and related reactive intermediates, which is brought about by oxidation of monophenols and benzenediols by proteins exhibiting tyrosinase activity, such as human tyrosinase and the related proteins TRP1 and TRP2. Although the substances and the produced reactive intermediates are toxic and can induce cell death, it is more relevant according to this invention that they function as haptens that become covalently bound to the tyrosinase enzymes, in particular to histidine moieties, in or near the catalytic site of proteins exhibiting tyrosinase activity, such as tyrosinase, TRP1 and TRP2. An immune response is then to be mounted against these haptenized auto-antigens, in order to treat... |
| Taste improving agent for food and beverage containing potassium chloride, process for producing food and beverage containing potassium chloride and food and beverage containing potassium chloride produced by the process | 20080193591 | 20080814 |
| A taste improving agent for food and beverage containing potassium chloride that can effectively relieve unpleasant tastes, such as bitter taste and harsh taste, attributed to potassium chloride without detriment to the flavor of the food and beverage; a process for producing a food and beverage containing potassium chloride of high palatability having the bitter taste and harsh taste of potassium chloride suppressed; and a food and beverage containing potassium chloride produced by the production process. Use is made of a taste improving agent comprising a basic amino acid and/or a basic peptide as an active ingredient. It is preferred that the basic amino acid be at least one member selected from among histidine, arginine and lysine and the basic peptide at least one member selected... |
| Compositions based on amino acids for improving the myocardial ventricular function in patients suffering from diabetes | 20080194665 | 20080814 |
| Compositions based on amino acids are described, for improving the myocardial ventricular function in patients suffering from diabetes, particularly but not exclusively II type diabetes. The compositions according to the invention comprise up to 75% of the branched chain amino acids leucine, isoleucine and valine, as active ingredients. Preferably, the compositions also comprise, as further active ingredients, up to 50% of threonine and lysine. Other essential amino acids are preferably also provided, in particular methionine, phenylalanine, histidine, tryphtophan, as well as non essential amino acids, in particular tyrosine and/or cyst(e)ine (i.e., cystine and cysteine). Other amino acids can be added, provided that their sum is in a percentage being lower than 20% with respect to the other active ingredients, and less than 10% for each single... |
| Stable liquid il-1 antagonist formulations | 20080188817 | 20080807 |
| Formulations of an interleukin-1 (IL-1) antagonist are provided including a pre-lyophilized formulation, a reconstituted lyophilized formulation, and a stable liquid formulation. Preferably, the IL-1 antagonist is an IL-1 trap composed of a dimer of two fusion proteins having an amino acid sequence of SEQ ID NO: 10. Stable liquid formulations made with and without sodium chloride, and made with phosphate or histidine buffer, are provided.
... |
| Combinatorial artificial receptors including peptide building blocks | 20080182270 | 20080731 |
| R6 can be hydrogen or any suitable blocking or protecting group for an carboxyl-terminal carboxyl group of a peptide. Suitable blocking or protecting groups include those described in Green, T W; Wuts, PGM (1999), Protective Groups in Organic Synthesis Third Edition, Wiley-Interscience, New York, 779 pp. In an embodiment, R6 is hydrogen. In an embodiment, R6 is —XR10, in which X is a heteroatom such as N, O, or S and R10 is lower (e.g., C1 to C6) alkyl, substituted lower (e.g., C1 to C6) alkyl, aryl, substituted aryl, or the like. In an embodiment, R6 is —NHCH3.
... |
| Metabotropic glutamate receptor activator | 20080182811 | 20080731 |
| Amino acids other than glutamic acid are used as a metabotropic glutamate receptor activator. More preferably, aspartic acid, valine and cysteine are used as a group I metabotropic glutamate receptor activator; alanine, arginine, asparagine, aspartic acid, cysteine, glutamine, glycine, histidine, isoleucine, leucine, lysine, methionine, phenylalanine, proline, serine, threonine, tryptophan, tyrosine, valine, ornithine, taurine and hydroxyproline are used as a group II metabotropic glutamate receptor activator; and cysteine is used as a group III metabotropic glutamate receptor activator.
... |
| Alkaline protease | 20080177040 | 20080724 |
| The present invention makes it possible to efficiently produce and provide alkaline proteases having activity even in the presence of a highly concentrated fatty acid, and exhibiting excellent detergency for the removal of a complex stain containing protein, sebum and the like, and therefore being useful as an enzyme to be incorporated in a detergent.
... |
| Use of a gene encoding a histidine protein kinase to create drought resistant plants | 20080178346 | 20080724 |
| Plant expression vectors that include promoter sequences operably linked to heterologous ATHK1 polynucleotides, or complements thereof, encoding polypeptides at least 95% identical to SEQ ID NO:26, where the polynucleotides encode polypeptides that confers drought resistance in the plants. Also provided are transgenic plants with increased drought resistance, methods for creating such plants, overexpressors, and underexpressors of ATHK1. Methods for enhancing drought resistance in plants are also provided.
... |
| Method and composition for treating or prevending an oral cavity | 20080170998 | 20080717 |
| The invention relates to a composition for treating or preventing an oral cavity by preventing adhesion of Porphyromonas gingivalis as periodontopathic bacterium to oral tissue. The invention also relates to a composition for treating or preventing an oral cavity containing a peptide in which arginine and histidine bind alternately. Preferably, the invention includes a composition for treating or preventing an oral cavity including the peptide of a pentamer of (arginine-histidine).
... |
| Vaccines comprising aluminum adjuvants and histidine | 20080160045 | 20080703 |
| To improve the stability of vaccines comprising aluminum salt(s), the invention uses the amino acid histidine. This can improve pH stability and adjuvant adsorption and can reduce antigen hydrolysis. Histidine is preferably present during adsorption to the aluminum salt(s). The antigen in the vaccine may be a protein or a saccharide and is preferably from N. meningitidis.
... |
| Use of l-2-thiohistidine or one of its derivatives as a depigmenting agent in cosmetics | 20080161377 | 20080703 |
| The invention relates to the use of L-2-thiohistidine, or a cosmetically acceptable salt or ester of its acid group, as a depigmenting agent in a cosmetic composition or for the preparation of a cosmetic composition. It further relates to a method of cosmetic care for toning down or eliminating pigment spots on the skin and/or lightening the complexion by the application of this cosmetic composition. The invention provides a highly depigmenting composition.
... |
| Methods and compositions for specifically targeting human hepatocellular carcinoma cells | 20080152650 | 20080626 |
| Particular aspects of the present invention provide methods and compositions for the targeting and/or treating hepatocellular carcinoma (HCC) cells to affect cancer cell growth or viability. Exemplary methods and compositions relate to cell-associated HCC proteins (e.g., SEQ ID NOS:1-8, corresponding to PGMRCI (prostaglandin receptor membrane component 1), SEMA5A (semaphorin 5A), SLC2A2 (solute carrier family member), ABCC2 (ATP-binding cassette subfamily C member 2) and HAL (histidine ammonia lyase)), and are based, at least in part, upon the discovery that specific target genes and/or gene products are up or down-regulated in diseased tissue relative to normal tissue or in tissue of patients having other ailments. Inventive compositions comprise, for example, antibodies, antisense and siRNA agents.
... |
| Endogenous peptide and active subfragments thereof | 20080125355 | 20080529 |
| The present invention relates to a substantially pure biologically active consecutive anti-angiogenic polypeptide comprising the central region of human Histidine Rich Glycoprotein (HRGP). Said polypeptide is shown to comprise a potential endogenous, naturally occurring subfragment of human HRGP, comprising similar anti-angiogenic activities as the mature protein. The present invention also relates to one or more new biologically active subfragments of human HRGP, derived from said central region. Said subfragments are all characterized by having anti-angiogenic activity. One of the active subfragments is referred to as Pep2. Enscoped by the present invention are also anti-angiogenic subfragments derived from Pep2, one of them comprising a newly identified presently minimal functional entity.
... |
| Catalytic conversion of carbonyl type compounds, including amides and others, to methyl ether polymers, substituted methyl ether polymers and methyl ether ladder polymers | 20080114150 | 20080515 |
| Catalytic processes have been developed for direct chemical conversion of aqueous carbonyl type compounds including amides, sulfoxides and related carbonyl type compounds to methyl ether polymers, substituted methyl ether polymers and/or substituted methyl ether ladder polymers. Amide and sulfoxide carbonyl type compounds including DMF, DMAc, MBAc, MEHx, amides prepared from an organic acid including serine, arginine, histidine and related amino acids, reacted with amines including monoethanolamine, butylamines, methylpropylamines and related amines and DMSO have been polymerized in an aqueous environment to methyl ether polymers, substituted methyl ether polymers or substituted methyl ether ladder polymers by this catalytic process. The catalysts are based on molecular strings of mono-, di- and tri-valent transition metal compounds. Laboratory results have demonstrated [cobalt(II)]2, [manganese(II)]2, cobalt(II)-manganese(II), [cobalt(III)]2 and related families of catalysts... |
| Therapeutic agent for inflammatory bowel disease and tnf-alfa production inhibitor | 20080108684 | 20080508 |
| Disclosed is an agent for use in the treatment or prevention of inflammatory bowel disease. Also disclosed is an agent for inhibiting the production of TNF-α. A therapeutic or prophylactic agent for inflammatory bowel disease comprising at least one amino acid selected from the group consisting of lysine, histidine, phenylalanine, methionine, tryptophan, glutamine, glycine, cysteine, cystine and threonine, the amino acid being administered at a dose of 0.1 to 4000 mg/kg per day; and a TNF-α production inhibitor comprising an amino acid selected from the group consisting of histidine, phenylalanine and tryptophan, the amino acid being administered at a dose of 0.1 to 4000 mg/kg per day.
... |
| Water-soluble elastin, process for producing same, and food and medicine containing same | 20080096812 | 20080424 |
| A low-molecular-weight water-soluble elastin having a molecular weight of about 10,000 to 30,000 and a high-molecular-weight water-soluble elastin having a molecular weight of about 30,000 to 300,000 are provided, 79% to 84% of the constituent amino acids of the elastin comprising proline, glycine, alanine, and valine, 2% to 3% comprising aspartic acid and glutamic acid, 0.7% to 1.3% comprising lysine, histidine, and arginine, and 0.2% to 0.4% comprising desmosine and isodesmosine. The low-molecular-weight water-soluble elastin that is obtained may be used in a functional food or a medicine. Such a high-purity water-soluble elastin may be produced by obtaining pure insoluble elastin by subjecting animal body tissue to a collagen removal treatment and then fragmenting the insoluble elastin by means of a solubilizing liquid. It may be... |
| Prophylactic/therapeutic agent for stress-induced bowel disease | 20080090749 | 20080417 |
| Provided are a prophylactic/therapeutic agent for a stress-induced bowel disease, containing, as an active ingredient, at least one kind selected from the group consisting of histidine, a peptide comprising histidine, a precursor thereof and a pharmacologically acceptable salt thereof, a food/beverage having prophylactic/ameliorating action on the disease, a suppressant of the release of a chemical transmitter during stress induction, and a food/beverage having suppressive action on the release of the transmitter.
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| Skin composition | 20080076808 | 20080327 |
| The present invention provides a composition preferably a pet foodstuff comprising pantothenic acid, nicotinamide, histidine, inositol and choline wherein pantothenic acid is provided at a level of 10 mg to 500 mg per 400 kcal per day, its use in the treatment of a skin disorder and methods of controlling a skin disorder. The invention further provides a method of manufacturing a composition of the invention.
... |
| Process for producing protein in cell-free protein synthesis system and reagent kit for protein synthesis | 20080076905 | 20080327 |
| This invention provides a process for producing an isotope-labeled protein used as a sample for protein 3D structural analysis via NMR in a cost-effective manner within a short period of time. In this process, a protein is synthesized using, as a substrate, an amino acid mixture that contains a maximum of 19 different types of amino acids selected from the group consisting of alanine, arginine, aspartic acid, cysteine, glutamic acid, glycine, histidine, isoleucine, leucine, lysine, methionine, phenylalanine, proline, serine, threonine, tryptophan, tyrosine, valine, asparagine, and glutamine in a cell-free protein synthesis system.
... |
| C-terminal modification of polypeptides | 20080064079 | 20080313 |
| The invention relates to a mutated trypsin comprising an amino acid substitution both at position K60 and D189, and at least one more amino acid substitution by histidine at position N143 or position E151. Such trypsin mutant has a preferred cleavage site comprising the amino acids Xaa1-Xaa2-His, wherein Xaa1 is L, Y or F and Xaa2 is R or K. The invention also relates to a man-made polypeptide comprising a target peptide and the above cleavage site as well as to a method of producing C-terminally modified target peptides by using this mutated trypsin.
... |
| Polymer particles | 20070299249 | 20071227 |
| A process for covalently binding a tagged protein to a polymer particle comprising: contacting a tagged protein with a chelating agent-polymer particle conjugate wherein said tag comprises at least two histidine residues and at least two lysine residues and said chelating agent is tridentate, tetradentate or pentadentate and comprises at least two carboxyl groups and is coordinated by Co2+ ions, to form particle-chelating agent Co2+ complex: contacting said complex with a carbodiimide; and optionally removing the Co2+ ions.
... |
| Method for reducing acrylamide formation in thermally processed foods | 20070292589 | 20071220 |
| In fabricated, thermally processed snack foods, the addition of one of a select group of amino acids to the recipe for the food inhibits the formation of acrylamide during the thermal processing. The amino acid can come from the group of cysteine, lysine, glycine, histidine, alanine, methionine, glutamic acid, aspartic acid, proline, phenylalanine, valine, and arginine and can be a commercially available amino acid or in a free form in an ingredient added to the food. Amino acids can be added to fabricated foods at the admix stage or by exposing raw food stock to a solution containing a concentration of the amino acid additive.
... |
| Amino acid compositions | 20070286909 | 20071213 |
| Compositions are described herein that are nutritional supplements that contain free amino acids. These supplements contain a homogenous mixture of free amino acids, wherein the free-form amino acids comprise L-Lysine, L-Valine, L-Tryptophan, L-Phenylalanine, L-methionine, L-Leucine, L-Threonine, L-Isoleucine, L-Arginine, L-Histidine, L-Tyrosine, L-Carnitine, L-Serine, L-Glutamine, Aspartic Acid, L-Proline, L-Glycine, Taurine, L-Cysteine, Gamma-aminobutyric acid (GABA), L-Alanine, L-Glutamic acid, and wherein the composition comprises at least one B vitamin. These compositions are of use to treat disorders associated with a deficiency at least one amino acid, such as soft tissue injury, insomnia, panic attacks, anxiety disorders, eating disorders, anorexia, depression, chronic pain, emotional distress, chemical dependence, alcoholism, and hypoglycemia.
... |
| Infusion fluid for dialysis patients | 20070281985 | 20071206 |
| A pharmaceutical preparation including an amino acid infusion fluid is administered to patients receiving dialysis to ameliorate nutritional status of patients. As a result, anemia can be ameliorated and the required dose of erythropoietin can be reduced in these patients. Furthermore, the serum phosphate levels can be controlled to a predetermined range and protein catabolism can be suppressed in such patients. The amino acid infusion fluid has at least one essential amino acid. The preferred amino acid composition includes at least L-isoleucine, L-leucine, L-lysine, L-methionine, L-phenylalanine, L-threonine, L-tryptophan, L-valine, L-alanine, L-arginine, L-aspartic acid, L-glutamic acid, L-histidine, L-proline, L-serine, L-tyrosine, glycine and L-cysteine, wherein the ratio of essential amino acids to non-essential amino acids is 2.5 or higher.
... |
| Thrombin derivatives and medicinal composition containing the same | 20070282095 | 20071206 |
| The present invention provides a thrombin derivative, comprising an A chain and a B chain, the B chain having an amino acid sequence in which one or more kinds of active center amino acids selected from the group consisting of serine at position 205, glycine at position 203, aspartic acid at position 99, and histidine at position 43 in an amino acid sequence of a thrombin B chain are substituted, having the properties: (1) cleaving a thrombin substrate at the ratio of 10% or less when it is reacted with the thrombin substrate in 50 mM Tris-HCl (pH 7.4) containing 0.1 M NaCl at 37° C. for 3 hours, and (2) maintaining a structure of exosite I.
... |
| Compositions and methods for the treatment of skin damage | 20070275084 | 20071129 |
| The present invention provides methods and compositions for use in cosmetic and dermatological formulations. In various embodiments of the present invention, compositions comprising beta-alanyl-L-histidine (carnosine) or derivatives or analogs thereof and basic milk factor (BMF) for prophylaxis and treatment of aged or photodamaged, or damaged, as in wounded or disrupted, skin.
... |
| Cationic peptides for sirna intracellular delivery | 20070275923 | 20071129 |
| What is described is a composition for delivery of a RNA molecule to a cell, comprising: a double stranded RNA (dsRNA) molecule of about 15 to about 40 base pairs; and a polynucleotide delivery-enhancing peptide, comprising a region of alternating lysine and histidine residues, or of alternating D and L forms of arginine.
... |
| Material for processed food for weight reduction diets and weight reduction dietary processed food using thereof | 20070269490 | 20071122 |
| The purpose of the invention is to provide a material for weight reduction diet food and the processed food using the same, that is a natural food product obtained from the materials eaten in everyday life, and very safe to the human body. There is provided a material for processed food for weight reduction diets, wherein active ingredients including histidine were extracted from Bonito essence. In addition, the present invention provides the material for processed food for weight reduction diets, wherein 12,000 mg-20,000 mg weight % of histidine is included. Furthermore, the processed food for weight reduction diets using the above-mentioned material for processed food for weight reduction diets is offered. As examples of such processed food, besides supplements in tablets and capsules soup stock powder,... |
| Sport drink containing amino acids and carbohydrates | 20070270355 | 20071122 |
| A composition includes a plurality of amino acids. The plurality of amino acids includes at least one essential amino acid and at least one non-essential amino acid. The plurality of amino acids also includes at least one branch-chain amino acid. The composition also includes a source of carbohydrates. The compositions also includes purified water. The plurality of amino acids comprises about 1 wt % of the composition. A composition includes a plurality of amino acids, sodium citrate, sodium chloride, potassium phosphate, flavoring, a source of carbohydrates, and purified water. In some embodiments of the composition, the plurality of amino acids includes alanine, arginine, aspartate, cystine, glutamine, glycine, histidine, isoleucine, leucine, lysine, methionine, phenylalanine, proline, serine, threonin, tryptophan, tyrosine, and valine.
... |
| Chelating monomers and polymers | 20070254378 | 20071101 |
| This invention provides chelating moieties that comprise an aryl group. Monomers that include the chelating moieties can be polymerized into chelating polymers. Chelating polymers are useful to chelate metals. Chelating polymers in the form of metal chelates are useful for binding analytes, such as polypeptides that comprise histidine residues. Chelating polymers can be includes in articles such as chips and chromatographic materials.
... |
| Compositions that include hemagglutinin, methods of making and methods of use thereof | 20070224205 | 20070927 |
| Compositions comprise a flagellin component or a Toll-like Receptor agonist component that is at least a portion of a flagellin or a Toll-like Receptor agonist, wherein the flagellin component or Toll-like Receptor agonist component includes at least one cysteine residue and whereby the flagellin component or Toll-like Receptor agonist component activates a Toll-like Receptor 5 or Toll-like Receptor. Compositions comprise a flagellin component that is at least a portion of a flagellin, wherein at least one lysine of the flagellin component has been substituted with at least one arginine, serine and histidine, whereby the flagellin component activates Toll-like Receptor 5. Compositions can further include an antigen, such as an influenza antigen, a flavivirus antigen, a pathogen-related antigen, a bacterial capsular antigen and a carrier protein. The... |
| Method for producing l-amino acids using bacterium of the enterobacteriaceae family | 20070212764 | 20070913 |
| There is disclosed a method for producing an L-amino acid, for example L-threonine, L-lysine, L-histidine, L-phenylalanine, L-arginine, L-tryptophan, or L-glutamic acid, using a bacterium of the Enterobacteriaceae family, wherein the bacterium has been modified to enhance an activity of N-acetylglucosamine permease encoded by the nagE gene.
... |
| Seasoning composition, seasoning material, and process for producing foods using the same | 20070184176 | 20070809 |
| Seasoning compositions which contain, with respect to 100 parts of potassium chloride, 1.5 to 70 parts by weight of histidine or its salt, 4 to 100 parts by weight of lysine or its salt, 2 to 100 parts by weight of sodium inosinate or sodium guanylate, 20 to 130 parts by weight of lactic acid or its salt, and 5 to 50 parts by weight of phosphoric acid or its salt; and seasoning materials which contain, with respect to 100 parts by weight of the seasoning composition, 1 to 100 parts by weight by solid content or powder content of a seafood extract/meat extract; can be used to prepare foods that are excellent in flavor such as favorableness of saltiness and depth and richness of taste... |
| Method for producing l-histidine using bacteria of enterobacteriaceae family | 20070184532 | 20070809 |
| A method is provided for producing L-histidine using bacterium of the Enterobacteriaceae family, wherein the L-amino acid productivity of said bacterium is enhanced by enhancing an activity of the transaldolase encoded by the talB gene.
... |
| pharmaceutical formulation | 20070179096 | 20070802 |
| The invention relates to aqueous pharmaceutical formulations comprising human growth hormone, histidine, poloxamer, phenol, and mannitol.
... |
| Compositions, methods, systems, and kits for affinity purification | 20070148721 | 20070628 |
| The invention provides a method of separating proteins and peptides of a sample comprising contacting the sample with a Pd coordination compound. The Pd coordination compound binds to sulfur and/or nitrogen groups and thus is useful for purifying biomolecules comprising cysteine, methionine, histidine amino acids or derivatized amino acids/residues comprising sulfur or nitrogen groups which bind to coordination sites on the Pd coordination compounds. The invention also relates to methods, systems and kits for using the Pd coordination compound.
... |
| Poly zinc finger proteins with improved linkers | 20070149770 | 20070628 |
| Polynucleotides encoding chimeric proteins, and methods for their production and use are disclosed. The chimeric proteins comprise a flexible linker between two zinc finger DNA-binding domains, wherein the linker contains eight or more amino acids between the second conserved histidine residue of the carboxy-terminal zinc finger of the first domain and the first conserved cysteine residue of the amino-terminal zinc finger of the second domain.
... |
| Method for cleaving proteins | 20070134757 | 20070614 |
| This, invention relates to a method for cleaving proteins or peptides at a specific site. According to the invention an amino acid sequence is constructed at a predetermined cleavage site and the protein or peptide is allowed to react with free metal ions in a buffer. The buffer further comprises a reducing or oxidizing agent for enhancing the cleavage. The amino acids in the amino acid sequence are selected from the group comprising histidine, lysine, tryptophan, arginine, tyrosine, phenylalanine, and cysteine.
... |
| Method of producing transgenic plants having improved amino acid composition and improved yielding | 20070130643 | 20070607 |
| The object of the present invention is to provide transgenic plants which accumulate free amino acids, particularly at least one amino acid selected from among glutamic acid, asparagine, aspartic acid, serine, threonine, alanine and histidine accumulated in a large amount, in the edible parts thereof, and a method of producing them are provided. The other object of the present invention is to provide a method of increasing the yielding of potato and to provide a transgenic potato of which yielding can be increased. In the present invention, a sequence encoding glutamate dehydrogenase (GDH) gene is introduced into a plant together with a suitable regulatory sequence to express it in a plant cell, and thereby the GDH gene is excessively expressed.
... |
| L-histidine in ophthalmic solutions | 20070110782 | 20070517 |
| The invention relates to an aqueous ophthalmic solution comprising 0.00001 to about 10.0 percent by weight L-histidine, 0.0001 to 3.0 percent by weight hydrogen peroxide, and optionally 0.1 to 500 parts per million of a preservative that provides superior preservative efficacy especially as against fungal microbes. These solutions may be employed in various ways including cleaning contact lenses, rinsing lenses while in the eye, storing lenses and in delivering active pharmaceutical agents to the eye.
... |
| Vancomycin formulations having reduced amount of histamine | 20070105757 | 20070510 |
| Vancomycin composition treated to remove histamine and a method of removing histamine from vancomycin. The invention also includes an isolated polynucleotide sequence including an isolated polynucleotide sequence of histidine decarboxylase from Amycolatopsis orientalis. The vancomycin composition of the present invention is used to redue the incidence of Red Man Syndrome, phlebitis, and hypotension.
... |
| Composition containing dipeptide of histidine and alanine for reducing uric acid and method for reducing uric acid using the dipeptide | 20070099846 | 20070503 |
| The present invention relates to a composition comprising an effective amount or an effective amount of one or more dipeptides consisting of histidine or the functional equivalent thereof and alanine or the functional equivalent thereof for reducing uric acid in a subject. The invention also provides a method for the treatment of gout or the amelioration of symptoms related to a high level of uric acid comprising the step of administering or applying the above-mentioned dipeptides to a subject.
... |
| "n and/or nalpha derivatized, metal and organic protected l-histidine for coupling to biomolecules for highly efficient labeling with [m(oh2)3 (co)3]+ by fac coordination" | 20070077195 | 20070405 |
| The present invention relates to novel histidine derivatives that can be used for the labeling of biomolecules with radioactive metal tricarbonyls. The new derivatives have a histidine that is derivatized at the Nε and at least protected at the Nα and optionally at the Nδ; or derivatized at the Nα and at least protected at the Nα and optionally at the Nδ; or derivatized at the Nε and Nα and at least protected at the Nα and optionally at the Nδ; or derivatized at the Nε; or derivatized at the Nα; or derivatized at the Nε and Nα; or at least protected at the Nα and optionally at the Nδ.
... |
| Composition for oral cavity | 20070071694 | 20070329 |
| The invention relates a composition for oral cavity for preventing adhesion of Porphyromonas gingivalis as periodontopathic bacterium to oral tissue. The invention also relates to a composition for oral cavity containing a peptide in which arginine and histidine bind alternately. Preferably, the invention includes a composition for oral cavity including the peptide of a pentamer of (arginine-histidine).
... |
| Drugs for treating diabetes | 20070071794 | 20070329 |
| The present invention provides an agent for recovering insulin secretion function which contains at least one of the amino acids selected from the group consisting of aspartic acid, cystine, serine, asparagine, isoleucine, histidine, hydroxyproline, glutamic acid, valine and salts thereof as an active ingredient; a functional food which contains the agent for recovering insulin secretion function; and a composition for treating diabetes which contains the amino acid(s) and a second diabetic drug as active ingredients. This agent for recovering insulin secretion function can be used as an oral therapeutic agent or functional food that is useful for treating, improving or preventing insulin secretion defects in Type II diabetes, borderline diabetes and other diseases, and side effects caused by administration of drugs.
... |
| Vaccine compositions comprising streptococcus pneumoniae polypeptides having selected structural motifs | 20070065458 | 20070322 |
| A vaccine composition is disclosed that comprises polypeptides and fragments of polypeptides containing histidine triad residues or coiled-coil regions, some of which polypeptides or fragments lie between 80 and 680 residues in length. Also disclosed are processes for preventing infection caused by S. pneumoniae comprising administering of vaccine compositions.
... |
| Therapeutic fibrin-derived peptides and uses thereof | 20070037749 | 20070215 |
| The invention relates to peptides having the general formula (I), or a salt or amide thereof, wherein R1 and R2 are either the same or different, wherein R1 and R2 are each selected from the group consisting of hydrogen and a saturated or unsaturated hydrocarbon residue, said residue having from 1 to 10 carbon atoms, wherein Z1 is selected from the group consisting of histidine and proline, wherein Z2 is selected from the group consisting of an arginine and a peptide comprising an initial arginine and having from 2 to 30 amino acids. The invention also relates to methods using the peptides of the present invention in the treatment of inflammation.
... |
| Immunoconjugate formulations | 20070031402 | 20070208 |
| The present invention provides an immunoconjugate formulation that is substantially free of particles, the immunoconjugate formulation comprising: an immunoconjugate and one or more excipients selected from the group consisting of: sucrose, polysorbate 20, polysorbate 80, cyclodextrin, dextrose, glycerol, polyethylene glycol, mannitol, sodium chloride, and an amino acid, wherein the formulation is a buffered aqueous solution having a pH of 4.5 to 7.6. The present invention also provides an immunoconjugate formulation that is substantially free of aggregates, the immunoconjugate formulation comprising: an immunoconjugate and one or more excipients selected from the group consisting of histidine, sucrose, glycine and sodium chloride, wherein the formulation is a buffered aqueous solution having a pH of 4.5 to 7.6. The present invention further provides an immunoconjugate formulation that is substantially free... |
| Charged sophorolipids and sophorolipid containing compounds | 20070027106 | 20070201 |
| optionally followed by acidolytic (treating with an acid) or hydrogenolytic deprotection (treating with a hydrogenolysis catalyst) which removes one of the groups R1 or R2 and replaces it with hydrogen. Also a sophorolipid containing composition containing a carrier and at least one sophorolipid described above.
... |
| Sulfur atom-free enzyme protein | 20070015241 | 20070118 |
| A sulfur atom-free enzyme protein retaining the activity of the original enzyme protein and having oxidation resistance wherein L-cystein and L-methionine residues of the enzyme protein are substituted with 18 types of L-amino acid residues: L-alanine; L-aspartic acid; L-glutamic acid; L-phenylalanine; L-glycine; L-histidine; L-isoleucine; L-lysine; L-leucine; L-asparagine; L-proline; L-glutamine; L-arginine; L-serine; L-threonine; L-valine; L-tyrosine; and L-tryptophan. A enzyme protein retaining the activity of the wild type enzyme while having antioxidation properties against oxidation by hydrogen peroxide, and the like and a process for producing the same.
... |
| Phex substrates and methods using same | 20060292657 | 20061228 |
| A fluorogenic PHEX substrate comprising a peptide unit; a fluorophore unit capable of conferring fluorescence on said substrate attached to an amino acid residue at a first end of the peptide unit; and a quencher unit capable of providing intrarnolecular quenching of said fluorescence attached to an amino acid residue at a second end of the peptide unit; the peptide unit having at least 6 amino acids residues including a sequence P2-P1-P1-P2, of 4 amino acid residues at positions P2, P1, P1, and P2 of the peptide unit, respectively; the amino acid residue at position P2 being any amino acid residue; the amino acid residue at position P, being any amino acid residue except an isoleucine, a valine, or a histidine residue; the amino acid residue... |
| Affinity membrane for capture of a target biomolecule and formation thereof by site-directed immobilization of a capture biomolecule | 20060292680 | 20061228 |
| Compositions and methods are taught for directing the orientation of an immobilized capture biomolecule on a hydrophobic membrane. The method comprises layering at least one tie layer on a hydrophobic membrane, adding an amine functional layer on top of at least one tie layer; and attaching an alignment biomolecule to the amine functional layer. The alignment biomolecule has the ability to either capture a target biomolecule itself and thus be considered a capture biomolecule, or bind and orient the immobilized capture biomolecule so as to maximize the binding activity of the immobilized capture biomolecule. In one embodiment, a nickel-coordinated amine functional layer binds with a histidine-tagged alignment biomolecule. In another embodiment, an amine functional layer reacts, via tyrosinase catalysis, with a tyrosine residue in an alignment... |
| Branched cationic copolymers and methods for antimicrobial use | 20060281683 | 20061214 |
| The invention provides a branched copolymer for the treatment of bacterial, fungal, and viral infections. The branched copolymer is characterized as having (i) at least 10 amino acids, (ii) at least 10% of the amino acids are histidine, (iii) at least 10% of the amino acids are non-histidine, (iv) said branched polymer comprising one or more backbones, (v) one or more terminal branches, and (vi) optionally, one or more non-terminal branches.
... |
| Histamine hyperproductive animal | 20060265772 | 20061123 |
| The invention of the present patent application provides, a histamine-hyperproductive animal, which is a non-human animal or progeny thereof obtained by ontogenesis of totipotent cells transfected with a polynucleotide encoding histidine decarboxylase and has the above polynucleotide in the cellular chromosome to produce histamine at a high level in the somatic cells. Thus, analysis of the pathogenesis and pathological consequence in various disorders associated with histamine in human as well as development of therapeutic techniques and remedies for these disorders will be developed.
... |
| Method of immobilizing a protein to a zeolite | 20060240567 | 20061026 |
| The present invention relates to a polypeptide tag and a method using said polypeptide tag sequence for immobilizing a protein on a microporous material, said microporous material is selected from the group consisting of zeolite or similar solid surfaces whereby loss of activity of said protein is less than 10% of the initial activity prior to immobilization, the method comprising the steps of: 1. Selecting a polypeptide tag capable of binding to the surface, 2. Immobilizing said protein by the steps of: attaching said polypeptide tag to the protein, and binding said polypeptide tag to the solid surface where step (a) and (b) is performed simultaneously or sequentially and when performed sequentially, the order of step (a) and (b) is random, subject to the limitation that... |
| Process for producing vitamin b6 | 20060216798 | 20060928 |
| Disclosed is a mutant of a recombinant microorganism of the genus Sinorhizobium capable of producing vitamin B6 having a recombinant plasmid with pdxJ gene that acquired histidine requirement of glycine resistance, or its combination thereof.
... |
| Stabilized liquid polypeptide formulations | 20060210557 | 20060921 |
| The present invention provides formulations for maintaining the stability of polypeptides, in particular, therapeutic antigen-binding polypeptides such as antibodies and the like, for example, anti-Aβ antibodies. The formulations generally include an antioxidant in a sufficient amount as to inhibit by-product formation, for example, the formation of high molecular weight polypeptide aggregates, low molecular weight polypeptide degradation fragments, and mixtures thereof. The formulations of the invention optionally comprise a tonicity agent, such as mannitol, and a buffering agent or amino acid such as histidine, and thus, the formulations are suitable for several different routes of administration.
... |
| Simplified eukaryotic nitrate reductase | 20060211084 | 20060921 |
| The invention provides modification to the polynucleotide coding sequence for Pichia angusta NAD (P)H: nitrate reductase [YNaR1; GenBank accession number Z49110], which has Enzyme Commission number 1.7.1.2 (formerly EC 1.6.6.2), yielding the polynucleotide coding sequence for simplified eukaryotic nitrate reductase (S-NaR1). The invention also provides a method for recombinant expression of said polynucleotide code in the cells of the methylotrophic yeast Pichia pastoris to produce the polypeptide for S-NaR1, which binds the host-produced molybdenum-molybdopterin cofactor and intracellularly forms catalytically active, nitrate-reducing enzyme as small and stable multimeric proteins. The invention also provides a method for rapid and high-yielding purification of S-NaR1 by utilizing the hexa-histidine sequence at the carboxyl-terminus of said polypeptide for immobilized metal affinity chromatography.
... |
| Skin composition | 20060204552 | 20060914 |
| The present invention provides a composition preferably a pet foodstuff comprising pantothenic acid, nicotinamide, histidine, inositol and choline wherein pantothenic acid is provided at a level of 10 mg to 500 mg per 400 kcal per day, its use in the treatment of a skin disorder and methods of controlling a skin disorder. The invention further provides a method of manufacturing a composition of the invention.
... |
| Streptoccal inhibitor of complement-mediated lysis, protein sic | 20060205925 | 20060914 |
| A protein from Streptococcus pyogenes, serotype M1 has been characterized. This protein, called protein SIC, plays a role in S. pyogenes pathogenicity and virulence. It inhibits hemolysis by interacting with the plasma proteins clusterin, and members of the cystatin protein super family such as histidine rich glycoprotein (HRG). The protein, comprises at least one of the following partial amino acid sequences: (a) glu thr tyr thr ser arg asn phe; (b) asp trp ser gly asp asp trp pro glu asp asp trp; (c) arg ser gly val gly leu ser gln tyr gly trp ser; (d) trp ser ser asp lys lys asp glu thr glu asp lys thr; (e) gly thr gly tyr glu lys arg asp asp trp gly gly pro gly; (f)... |
| Anti a beta antibody formulation | 20060193850 | 20060831 |
| The present invention provides formulations for maintaining the stability of Aβ binding polypeptides, for example, Aβ antibodies. Exemplary formulations include a tonicity agent such as mannitol and a buffering agent or amino acid such as histidine. Other exemplary formulations include an antioxidant in a sufficient amount as to inhibit by-product formation, for example, the formation of high molecular weight polypeptide aggregates, low molecular weight polypeptide degradation fragments, and mixtures thereof. The formulations of the invention optionally comprise a tonicity agent, such as mannitol, and a buffering agent or amino acid such as histidine. The formulations are suitable for several different routes of administration.
... |
| Radiosensitizer formulations and methods for use | 20060193917 | 20060831 |
| The present invention provides radiosensitizer compositions, in controlled-release formulations or other acceptable formulations, particularly nitrohistidine radiosensitizer compositions, which may be administered by any suitable means including oral, intravenous, arterial infusion, intraperitoneal, intramuscular, subcutaneous, surgical, and topical. Optionally, radiosensitizer compositions may be formulated with other agents, including chemotherapy agents and agents that provide a synergistic radiosensitizing effect. Methods of potentiating radiotherapy cancer treatment of cancers in humans, particularly of astrocytomas, are also presented, wherein a radiosensitizer composition is administered and radiotherapy is directed to the site of the tumor. Chemotherapy regimens may also be used as adjuvant therapy.
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| Method for producing amino acids by fermentation | 20060194302 | 20060831 |
| The present invention provides a method for producing an amino acid selected from the group consisting of L-alanine, L-valine, L-leucine, L-isoleucine, L-methionine, L-phenylalanine, L-proline, glycine, L-serine, L-threonine, L-cysteine, L-tyrosine, L-asparagine, L-glutamine, L-lysine, L-histidine, L-arginine, L-aspartic acid and L-glutamic acid and useful as medicament, chemical agent, food material and feed additive at high industrial efficiency, the method comprising culturing a microorganism having an ability to produce the amino acid and having resistance to an aminoquinoline derivative in a medium, producing and accumulating the amino acid in the present invention in the culture, and recovering the amino acid from the culture.
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| Culture media compositions free of fetal bovine serum | 20060194322 | 20060831 |
| A cell culture growth media free of Fetal Bovine Serum for use with parasitic organisms. The media includes calcium chloride, sodium bicarbonate, potassium chloride, sodium chloride, monosodium phosphate, glucose, hepes, ferric nitrate, magnesium sulfate, tricine, d-ribose, 2-deoxy ribose, adenosine-5-triphosphate (ATP), 2-deoxyadenylic acid (d-AMP), 5′-thymidylic acid (TMP), 2′-deoxyicitidine-5 monophosphate (d, 2′-deoxyuridine-5-monophosphate (d, 2′-deoxyguanilic Acid (d-GMP), aspartic acid, glutamic acid, 1-alanine, arginine, camosine, cysteine, cystine, glutamine, glycine, histidine, iso-leucine, leucine, lysine, methionine, omitine, phenylalanine, proline, serine, threonine, tryptophan, tyrosine, valine, ascorbic acid, biotine (H), camitine, cholecalciferol, choline chloride, cyanocobalamine (B12), ergocalciferol, folic acid, myo-inositol, menadione, nicotinamide, PABA, panthotenato, pyridoxal, pyridoxamine, pyridoxine, retinol (A), riboflavine (B2), Thiamine (B1), 6,8 Thiotic acid, alfa-tocoferol, 3-phytylnenadione (K1), tetrahydrofolic acid, hemin from procine, and nanopure water.
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| Buffered formulations for concentrating antibodies and methods of use thereof | 20060182740 | 20060817 |
| The present invention provides a method for producing a concentrated antibody preparation that includes the steps of: (a) obtaining an initial antibody preparation that is an aqueous solution of antibodies and histidine or acetate buffer at a concentration in the range of from about 2 mM to about 48 mM; and (b) subjecting the antibody preparation to membrane filtration so as to remove water and buffer but not antibodies from the antibody preparation, thereby producing an antibody preparation having a higher concentration of antibodies than the initial antibody preparation. The concentrated antibody preparations produced by the method have lower viscosity and are more stable than those of other formulations. The invention further includes concentrated antibody preparations produced by the method, pharmaceutical compositions made using such preparations,... |
| Thioester-terminated water soluble polymers and method of modifying the n-terminus of a polypeptide therewith | 20060178505 | 20060810 |
| The invention provides reagents and methods for conjugating a polymer specifically to the α-amine of a polypeptide. The invention provides monofunctional, bifunctional, and multifunctional PEGs and related polymers having a terminal thioester moiety capable of specifically conjugating to the α-amine of a polypeptide having a cysteine or histidine residue at the N-terminus. The invention provides reactive thioester-terminated PEG polymers that have suitable reactivity with an N-terminal cysteine or histidine residue of a polypeptide to produce an amide bond between the PEG molecule and the polypeptide.
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| Use of protein histidine phosphatase | 20060153825 | 20060713 |
| The invention relates to the use of polypeptides with protein histidine phosphatase activity derived from mammalians, antibodies directed against them and DNA or RNA sequences complementary to mRNA sequences encoding polypeptides with protein histidine phosphatase activity for the modulation of ATP-citrate lyase and treatment of correlated pathophysiologic functions.
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| Engineering redox proteins | 20060148026 | 20060706 |
| The protein of this invention comprises a 4-α-helix bundle motif formed from the α-helices of rop (repressor of primer) and a redox centre. In this invention the redox centre is preferably haem and the iron is preferably coordinated to the α-helices of the rop structure via histidine residues. Such a protein is very stable and has the same specific activities as natural redox proteins with the increased stability in the interaction with electrode surfaces. Also provided by this invention is a method of engineering proteins to develop redox proteins from structures which previously had no redox functions.
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| Site-specific labeling of affinity tags in fusion proteins | 20060141554 | 20060629 |
| The present invention provides methods and fluorescent compounds that facilitate detecting and labeling of a fusion protein by being capable of selectively binding to an affinity tag. The fluorescent compounds have the general formula A(B)n, wherein A is a fluorophore, B is a binding domain that is a charged chemical moiety, a protein or fragment thereof and n is an integer from 1-6 with the proviso that the protein or fragment thereof not be an antibody or generated from an antibody. The present invention provides specific fluorescent compounds and methods used to detect and label fusion proteins that contain a poly-histidine affinity tag. These compounds have the general formula A(L)m(B)n wherein A is a fluorophore, L is a linker, B is an acetic acid binding domain,... |
| Method for producing l-amino acids using bacteria of the enterobacteriaceae family | 20060141586 | 20060629 |
| There is disclosed a method for producing an L-amino acid, for example L-threonine, L-lysine, L-histidine, L-phenylalanine, L-arginine, L-tryptophan or L-glutamic acid, using a bacterium of the Enterobacteriaceae family, wherein the bacterium has been modified to enhance an activity of L-arabinose permease.
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| Peptides and methods for the control of obesity | 20060135436 | 20060622 |
| wherein: X1 is an acyl group, Z is amino-2-naphthyl-carboxylic acid or histidine, Q is (D)phenylalanine or p-iodo-(D)phenylalanine, or a pharmacologically acceptable salt, complex or derivative thereof, the peptide derivative having melanocortin-4 receptor agonist activity.
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| Cytokinin-sensing histidine kinases and methods of use | 20060137033 | 20060622 |
| Isolated polynucleotides that encode cytokinin-sensing histidine kinase polypeptides, and the encoded polypeptides, are described. Expression cassettes comprising the polynucleotides of the invention and plants and plant cells that are transformed with the polynucleotides are described. Methods of using the cytokinin-sensing histidine kinase polypeptides and polynucleotides to modulate histidine kinase activity and/or histidine kinase levels in plants and plant cells are further described.
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| L-histidine in ophthalmic solutions | 20060127496 | 20060615 |
| The invention relates to an aqueous ophthalmic solution comprising 0.01 to about 1.0 percent by weight L-histidine; 0.01 to 0.0001 percent by weight hydrogen peroxide; 0.1 to 500 parts per million of a cationic polymeric preservative that provides superior preservative efficacy especially as against fungal microbes. These solutions may be employed in various ways including cleaning contact lenses, rinsing lenses while in the eye, storing lenses and in delivering active pharmaceutical agents to the eye.
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| Antimicrobial peptides with reduced hemolysis and methods of their use | 20060128614 | 20060615 |
| The present invention provides novel cyclic and linear short peptides containing one of the following amino acid residue sequences: Xa1-Naa-Xa1-Xa1-Naa-Xa2 or Xa1-Naa-Xa2-Xa1-Naa-Xa1 wherein: Xa1 represents lysine, arginine, or histidine; Naa represents an unnatural hydrophobic aromatic amino acid moiety selected from the group consisting of (naphtha-1-yl)alanine (1-Nal), (naphtha-2-yl)alanine (2-Nal), (benzothien-3-yl)alanine (Bal), diphenylalanine (Dip), (4,4′-biphen-yl)alanine (Bip), (anthracen-9-yl)alanine (Ath), and (2,5,7-tri-tert-butyl-indol-3-yl)alanine (Tht); and Xa2 represents valine, leucine, or isoleucine. The novel peptides exhibit broad spectrum antimicrobial activity against Gram-positive and Gram-negative bacteria and fungi by effecting modification of the primary peptide structure. Further, the peptides exhibit improved serum compatibility and reduced hemolysis.
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| Amino acid composition for improving central functions | 20060128778 | 20060615 |
| An amino acid composition or an amino acid solution for improving central functions which contains threonine, proline, glycine, valine, isoleucine, leucine, tyrosine, phenylalanine, lysine, aspartic acid, serine, glutamic acid, alanine, methionine, tryptophan, histidine and arginine; and an amino acid composition or an amino acid solution derived from the above composition by removing tryptophan. These amino acid compositions have effects of improving central functions such as healing fatigue, originate from natural materials and have substantially no side effect.
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| Processes of making and using pharmaceutical formulations of antineoplastic agents | 20060122163 | 20060608 |
| In its several embodiments, this invention discloses a pharmaceutical formulation comprising at least one antineoplastic agent or a pharmaceutically acceptable salt thereof, and at least one dissolution enhancing agent sufficient to substantially dissolve said at least one antineoplastic agent in at least one aqueous diluent, wherein said dissolution enhancing agent is urea, L-histidine, L-threonine, L-asparagine, L-serine, L-glutamine or mixtures thereof; a lyophilized powder comprising said pharmaceutical formulation, and articles of manufacture thereof.
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| Blood-viscosity reducing agent | 20060105071 | 20060518 |
| A blood-viscosity reducing agent contains a protein derived from Bacillus subtilis natto and including, sequentially from an amino group terminal, a first structural amino acid sequence having alanine, threonine, aspartic acid, glycine, valine, glutamic acid, tryptophan, asparagine, valine, aspartic acid, glutamine, isoleucine, aspartic acid, alanine, proline, lysine, alanine, tryptophan, alanine, leucine, glycine, tyrosine aspartic, acid, glycine, threonine, glycine, threonine, valine, valine, alanine, serine, isoleucine, aspartic acid, threonine, glycine, valine, glutamic acid, tryptophan, asparagine, histidine, proline, alanine, leucine, lysine, glutamic acid, lysine, tyrosine, arginine, glycine, tyrosine, asparagine, proline, glutamic acid, asparagine, proline, asparagine, glutamic acid, proline, glutamic acid, asparagine, glutamic acid, methionine, asparagine, tryptophan, tyrosine, aspartic acid, alanine, valine, alanine, glycine, glutamic acid, alanine, serine, proline, tyrosine, aspartic acid, aspartic acid, leucine, alanine, histidine, glycine, threonine, histidine,... |
| Fluorescence polarization assay for determining histidine decarboxylase activity | 20060105404 | 20060518 |
| A fluorescence polarization assay for determining the HDC modulating activity of a candidate compound comprising the steps of: a) providing a reaction mixture comprising a HDC, histidine, a fluorescently labeled histamine probe, a candidate compound and an anti histamine antibody having selectivity for histamine at least 10 fold greater than histidine; b) incubating the reaction mixture; c) determining whether inhibition of HDC has occurred in the presence of the test compound, wherein an increase in fluorescence signal is an indication that the test compound inhibits the activity of the HDC.
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| Antibody formulations | 20060088523 | 20060427 |
| The present application describes antibody formulations, including monoclonal antibodies formulated in histidine-acetate buffer, as well as a formulation comprising an antibody that binds to domain II of HER2 (for example, Pertuzumab), and a formulation comprising an antibody that binds to DR5 (for example, Apomab).
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| Method for producing l-amino acids using bacteria of the enterobacteriaceae family | 20060088919 | 20060427 |
| There is disclosed a method for producing L-amino acid, for example L-threonine, L-lysine, L-histidine, L-phenylalanine, L-arginine or L-glutamic acid, using a bacterium of the Enterobacteriaceae family, wherein the bacterium has been modified to enhance an activity of D-xylose permease.
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