Acting On Nitrogen-containing Compound As Donor (1.2, 1.5, 1.7) Patents (Class 435/191)
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Publication number: 20130273023Abstract: The present invention provides for the identification, isolation and uses of mammalian Monoamine Oxidase C (MAO-C), also known as renalase.Type: ApplicationFiled: April 21, 2011Publication date: October 17, 2013Applicant: YALE UNIVERSITYInventors: JIANCHAO XU, GARY DESIR
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Publication number: 20130267007Abstract: This invention provides an amadoriase having high substrate specificity to fructosyl valyl histidine. Such amadoriase comprises substitution of one or more amino acid residues at positions corresponding to amino acids selected from the group consisting of position 98, position 259, position 154, position 125, position 261, position 263, position 106, position 103, position 355, position 96, position 66, position 67, position 70, position 100, position 110, position 113, position 114, and position 156 in the amadoriase derived from the genus Coniochaeta. This invention enables accurate measurement of ?-fructosyl valyl histidine derived from the ?-chain amino terminus in glycated hemoglobin in the presence of ?-fructosyl lysine.Type: ApplicationFiled: August 4, 2011Publication date: October 10, 2013Inventors: Atsushi Ichiyanagi, Kozo Hirokawa, Yasuko Tanabe, Yosuke Masakari
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Publication number: 20130152231Abstract: The present invention provides methods and compositions relating to altering NT activity, nitrogen utilization and/or uptake in plants. The invention relates to a method for the production of plants with maintained or increased yield under low or normal nitrogen fertility. The invention provides isolated nitrate transporter (NT) nucleic acids and their encoded proteins. The invention further provides recombinant expression cassettes, host cells, and transgenic plants. Plants transformed with nucleotide sequences encoding the NT enzyme show improved properties, for example, increased yield.Type: ApplicationFiled: February 19, 2013Publication date: June 13, 2013Applicant: PIONEER HI-BRED INTERNATIONAL, INC.Inventor: Pioneer Hi-Bred International, Inc.
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Publication number: 20130129767Abstract: The present invention relates to specific regions of the N-terminal portion of the VAR2CSA protein and to the use of such specific regions in the prevention of pregnancy-associated malaria. The invention also provides immunogenic compositions and vaccines that are useful for preventing malaria in pregnant women.Type: ApplicationFiled: July 29, 2011Publication date: May 23, 2013Applicant: INSTITUT DE RECHERCHE POUR LE DEVELOPPEMENT (IRD)Inventors: Nicaise Tuikue Ndam, Philippe Deloron, Sedami Ursula Alix Carine Gnidéhou, Mickaël Quiviger, Pascal Bigey, Daniel Scherman
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Publication number: 20130108607Abstract: The subject invention relates in one aspect to an oxalate degrading composition, which includes at least one oxalate degrading enzyme. The composition includes an enriched insoluble component of fungal biosample, and the composition is effective to degrade oxalate at a pH of 1.9 or higher. The composition is protected from protease degradation such as pepsin, trypsin and chymotrypsin. The composition is capable of withstanding the conditions of the stomach, small intestines, and/or large intestines of a subject.Type: ApplicationFiled: November 23, 2010Publication date: May 2, 2013Inventors: Aaron Cowley, Qing-Shan Li
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Patent number: 8431122Abstract: The present invention comprises methods and compositions for the reduction of oxalate in humans, and methods for the purification and isolation of recombinant oxalate reducing enzyme proteins. The invention provides methods and compositions for the delivery of oxalate-reducing enzymes in particle compositions. The compositions of the present invention are suitable in methods of treatment or prevention of oxalate-related conditions.Type: GrantFiled: July 2, 2009Date of Patent: April 30, 2013Assignee: Oxthera Intellectual Property ABInventors: Harmeet Sidhu, Qingshan Li, Aaron Blake Cowley, Carl-Gustaf Golander
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Publication number: 20130101571Abstract: Methods and compositions for detoxifying nitrobenzodiazepines with nitroreductase mutants.Type: ApplicationFiled: March 23, 2012Publication date: April 25, 2013Applicant: Academia SinicaInventors: Andrew H-J. Wang, Shiuan-Woei Lin Wu, Fu-Chuo Peng, Che-An Wu
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Publication number: 20130089535Abstract: Disclosed herein is a novel enzymatic agent effective in reducing acetaldehyde in the oral cavity. It has been found that an aldehyde dehydrogenase derived from a microorganism belonging to the genus Saccharomyces and a threonine aldolase derived from Escherichia coli are effective in reducing low concentrations of acetaldehyde. Therefore, an agent for reducing acetaldehyde in the oral cavity is provided, which contains these enzymes as active ingredients.Type: ApplicationFiled: June 7, 2011Publication date: April 11, 2013Applicant: AMANO ENZYME INC.Inventors: Kan Yamashiro, Takahumi Koyama
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Publication number: 20130091605Abstract: The NR enzymes described herein were discovered in the red algae of Porphyra perforata (PpNR) and Porphyra yezoensis (PyNR). The present invention provides methods and compositions relating to altering NR activity, nitrogen utilization and/or uptake in plants. The invention relates to a method for the production of plants with maintained or increased yield under low nitrogen fertility. The invention provides isolated nitrate reductase (NR) nucleic acids and their encoded proteins. The invention further provides recombinant expression cassettes, host cells, and transgenic plants. Plants transformed with nucleotide sequences encoding the NR enzyme show improved properties, for example, increased yield and growth.Type: ApplicationFiled: July 19, 2012Publication date: April 11, 2013Applicant: PIONEER HI BRED INTERNATIONAL INCInventors: Dale F. Loussaert, Dennis O'Neill, Carl R. Simmons, Haiyin Wang
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Publication number: 20130058911Abstract: The present invention is intended to provide a reducing agent effective for color development of meat and uses therefor. The present invention provides a reducing agent containing a heme reductase derived from a microorganism belonging to the genus Bacillus. Preferably, crushed bacterial cells of Bacillus subtilis, Bacillus amyloliquefaciens, Bacillus natto, Bacillus thuringiensis, or Bacillus mycoides are used.Type: ApplicationFiled: May 9, 2011Publication date: March 7, 2013Applicant: AMANO ENZYME INC.Inventors: Keita Okuda, Shotaro Yamaguchi
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Publication number: 20130052677Abstract: A naturally occurring or recombinant urate oxidase (uricase) covalently coupled to poly(ethylene glycol) or poly(ethylene oxide) (both referred to as PEG), wherein an average of 2 to 10 strands of PEG are conjugated to each uricase subunit and the PEG has an average molecular weight between about 5 kDa and 100 kDa. The resulting PEG-uricase conjugates are substantially non-immunogenic and retain at least 75% of the uricolytic activity of the unmodified enzyme.Type: ApplicationFiled: April 8, 2011Publication date: February 28, 2013Inventors: L. David WILLIAMS, Michael S. Hershfield, Susan J. Kelly, Mark G.P. Saifer, Merry R. Sherman
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Patent number: 8377672Abstract: Ligand functionalized substrates, methods of making ligand functionalized substrates, and methods of using functionalized substrates are disclosed.Type: GrantFiled: January 7, 2011Date of Patent: February 19, 2013Assignee: 3M Innovative Properties CompanyInventors: Jerald K. Rasmussen, Catherine A. Bothof, Kannan Seshadri, Erin A. Satterwhite, Robert T. Fitzsimons, James I. Hembre, Mahfuza B. Ali
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Publication number: 20130029378Abstract: The invention provides an isolated formate dehydrogenase (FDH) polypeptide specific for NADP+ and an isolated FDH polypeptide having an adenine ribose recognition loop comprising a first large amino acid and a second amino acid, wherein the first and second amino acid are arranged in space to allow the second amino acid to bond with a phosphate group. Also provided is a variant of an BAD+ specific FDH polypeptide, wherein the adenine ribose recognition loop has been mutated at least one position to alter the three dimensional polypeptide structure of the adenine ribose recognition loop to allow a phosphate group to be recognised. The polypeptides of the invention can be used in the conversion of NADP+ to NADP or in the conversion of BAD+ to NASH.Type: ApplicationFiled: October 6, 2009Publication date: January 31, 2013Applicant: ISIS INNOVATION LIMITEDInventors: Benjamin Guy Davis, Ayhan Celik, Gideon John Davies, Karen Mary Ruane
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Patent number: 8361761Abstract: A process for production of cyclopropyl-fused pyrrolidine-based inhibitors of dipeptidyl peptidase IV is provided which employs a BOC-protected amine of the structure prepared by subjecting an acid of the structure to reduce amination by treating the acid with ammonium formate, nicotinamide adenine dinucleotide, dithiothreitol and partially purified phenylalanine dehydrogenase/formate dehydrogenase enzyme concentrate (PDH/FDH) and without isolating treating the resulting amine of the structure 2 with di-tert-butyl dicarbonate to form the BOC-protected amine.Type: GrantFiled: June 14, 2012Date of Patent: January 29, 2013Assignee: Bristol Myers-Squibb CompanyInventors: Michael Politino, Matthew M. Cadin, Paul M. Skonezny, Jason G. Chen
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Publication number: 20130017169Abstract: Multimeric protein structures are disclosed herein, as well a process for preparing same, and methods employing same for treating various diseases or disorders. The multimeric protein structures comprise at least two monomers of a therapeutic protein, including a TNF-alpha, a luteinizing hormone, an immunoglobin, a TNF-alpha receptor, a CTLA-4, a urate oxidase, a VEGF, a PDGF, a VEGF receptor, a PDGF receptor, an interleukin-17, and/or fragments thereof, the monomers being covalently linked to one another via a linking moiety. The multimeric protein structures exhibit improved performance as compared to the corresponding native proteins, including a longer lasting activity in vivo.Type: ApplicationFiled: March 2, 2011Publication date: January 17, 2013Applicant: PROTALIX LTD.Inventors: Ilya Ruderfer, Orit Shilovittzky, Avidor Shulman, Joseph Shaaltiel, Tehila Ben-Moshe, Talia Shekhter, Yaniv Azulay
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Publication number: 20130014291Abstract: Methods and compositions for modulating plant development are provided. Polynucleotide sequences and amino acid sequences encoding cytokinin oxidase polypeptides are provided. The sequences can be used in a variety of methods including modulating root development, modulating floral development, modulating leaf and/or shoot development, modulating seed size and/or weight, modulating tolerance under abiotic stress, and modulating resistance to pathogens. Polynucleotides comprising CKX promoters are also provided. The promoters can be used to regulate expression of a sequence of interest. Transformed plants, plant cells, tissues, and seed are also provided.Type: ApplicationFiled: June 12, 2012Publication date: January 10, 2013Applicant: Pioneer Hi Bred International Inc.Inventors: Norbert Brugiére, Jeffrey E. Habben
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Patent number: 8323942Abstract: The present invention is directed to methods for inducing desired activity in enzymes or microorganisms capable of producing the enzymes. The invention is further directed to methods of stabilizing activity in microorganisms. In specific embodiments, the invention provides methods for inducing and stabilizing nitrile hydratase activity, amidase activity, and asparaginase I activity. The invention further provides compositions comprising enzymes or microorganisms having induced and/or stabilized activity.Type: GrantFiled: April 3, 2009Date of Patent: December 4, 2012Assignee: Georgia State University Research FoundationInventors: George E. Pierce, Gene K. Drago, Sangeeta Ganguly
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Publication number: 20120269795Abstract: The present invention provides a humanized recombinant uricase and mutants thereof, wherein the humanized recombinant uricase is a chimeric protein which comprises amino acids of non-human mammal uricase and amino acids of human uricase. The humanized recombinant unease and mutants thereof have reduced immunogenicity in human, and can be used for the treatment of hyperuricemia and gout.Type: ApplicationFiled: March 12, 2010Publication date: October 25, 2012Applicant: Congqing Fagen Biomedical Inc.Inventors: Kai Fan, Chun Zhang, Xuefeng Ma, Xiang Mei, Chunlan Hu
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Publication number: 20120266329Abstract: The invention provides polypeptides, including enzymes, structural proteins and binding proteins, polynucleotides encoding these polypeptides, and methods of making and using these polynucleotides and polypeptides. Polypeptides, including enzymes and antibodies, and nucleic acids of the invention can be used in industrial, experimental, food and feed processing, nutritional and pharmaceutical applications, e.g., for food and feed supplements, colorants, neutraceuticals, cosmetic and pharmaceutical needs.Type: ApplicationFiled: February 20, 2012Publication date: October 18, 2012Applicant: BP Corporation North America Inc.Inventors: Eric J. Mathur, Cathy Chang
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Publication number: 20120264179Abstract: The invention provides a non-naturally occurring microbial organism having an adipate, 6-aminocaproic acid or caprolactam pathway. The microbial organism contains at least one exogenous nucleic acid encoding an enzyme in the respective adipate, 6-aminocaproic acid or caprolactam pathway. The invention additionally provides a method for producing adipate, 6-aminocaproic acid or caprolactam. The method can include culturing an adipate, 6-aminocaproic acid or caprolactam producing microbial organism, where the microbial organism expresses at least one exogenous nucleic acid encoding an adipate, 6-aminocaproic acid or caprolactam pathway enzyme in a sufficient amount to produce the respective product, under conditions and for a sufficient period of time to produce adipate, 6-aminocaproic acid or caprolactam.Type: ApplicationFiled: April 20, 2012Publication date: October 18, 2012Applicant: GENOMATICA, INC.Inventors: Anthony P. Burgard, Priti Pharkya, Robin E. Osterhout
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Publication number: 20120244138Abstract: Methods and compositions for detoxifying nitrobenzodiazepines with nitroreductase mutants.Type: ApplicationFiled: March 23, 2012Publication date: September 27, 2012Applicant: Academia SinicaInventors: Andrew H-J. Wang, Shiuan-Woei Lin Wu, Fu-Chuo Peng, Che-An Wu
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Publication number: 20120220011Abstract: The present invention provides unstructured recombinant polymers (URPs) and proteins containing one or more of the URPs. The present invention also provides microproteins, toxins and other related proteinaceous entities, as well as genetic packages displaying these entities. The present invention also provides recombinant polypeptides including vectors encoding the subject proteinaceous entities, as well as host cells comprising the vectors. The subject compositions have a variety of utilities including a range of pharmaceutical applications.Type: ApplicationFiled: February 14, 2012Publication date: August 30, 2012Applicant: Amunix Operating Inc.Inventors: Volker Schellenberger, Willem P. Stemmer, Chia-wei Wang, Michael D. Scholle, Mikhail Popkov, Nathaniel C. Gordon, Andreas Crameri
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Publication number: 20120208226Abstract: In one form, a mutant fructosyl amino acid oxidase modified at an amino acid residue involved in a proton relay system is provided. The mutant fructosyl amino acid oxidase has reduced oxidase activity while substantially maintaining its dehydrogenase activity. Other forms include an assay device and assay method for measuring glycated protein. Still, other forms include unique methods, techniques, systems and devices involving a mutant fructosyl amino acid oxidase.Type: ApplicationFiled: February 3, 2012Publication date: August 16, 2012Inventors: Kazunori Ikebukuro, Sode Koji
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Publication number: 20120202235Abstract: In one form, a fructosyl peptidyl oxidase derived from a budding yeast Phaeosphaeria nodorum for assaying a glycated protein in a sample is provided. The fructosyl peptidyl oxidase has higher activity toward fructosyl valine as well as fructosyl valyl histidine, and may be useful in assaying HbA1c with higher sensitivity and specificity. Still, other forms include unique methods, techniques, systems and devices involving a fructosyl peptidyl oxidase.Type: ApplicationFiled: February 3, 2012Publication date: August 9, 2012Inventors: Kazunori Ikebukuro, Sode Koji
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Patent number: 8222009Abstract: A process for production of cyclopropyl-fused pyrrolidine-based inhibitors of dipeptidyl peptidase IV is provided which employs a BOC-protected amine of the structure prepared by subjecting an acid of the structure to reduce amination by treating the acid with ammonium formate, nicotinamide adenine dinucleotide, dithiothreitol and partially purified phenylalanine dehydrogenase/formate dehydrogenase enzyme concentrate (PDH/FDH) and without isolating treating the resulting amine of the structure 2 with di-tert-butyl dicarbonate to form the BOC-protected amine.Type: GrantFiled: June 17, 2010Date of Patent: July 17, 2012Assignee: Bristol-Myers Squibb CompanyInventors: Michael Politino, Matthew M. Cadin, Paul M. Skonezny, Jason G. Chen
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Publication number: 20120178168Abstract: Methods and compositions for the rapid and reversible destabilizing of specific proteins using cell-permeable, synthetic molecules are described. Stability-affecting proteins, e.g., derived from FKBP and DHFR proteins are fused to a protein of interest and the presence or absence of the ligand is used to modulate the stability of the fusion protein.Type: ApplicationFiled: March 22, 2012Publication date: July 12, 2012Applicant: THE BOARD OF TRUSTEES OF THE LELAND STANFORD JUNIOR UNIVERSITYInventors: Thomas J. Wandless, Laura Anne Banaszynski, Mari Iwamoto, Lystranne Alysia Maynard, Ling-chun Chen
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Publication number: 20120149083Abstract: A naturally occurring or recombinant urate oxidase (uricase) covalently coupled to poly(ethylene glycol) or poly(ethylene oxide) (both referred to as PEG), wherein an average of 2 to 10 strands of PEG are conjugated to each uricase subunit and the PEG has an average molecular weight between about 5 kDa and 100 kDa. The resulting PEG-uricase conjugates are substantially non-immunogenic and retain at least 75% of the uricolytic activity of the unmodified enzyme.Type: ApplicationFiled: November 29, 2011Publication date: June 14, 2012Applicants: Duke University, Mountain View Pharmaceuticals, Inc.Inventors: L. David Williams, Michael S. Hershfield, Susan J. Kelly, Mark G.P. Saifer, Merry R. Sherman
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Publication number: 20120144511Abstract: The invention relates to muteins of the pyrroline-5-carboxylate reductase 1 (PYCR1), to nucleic acid molecules comprising a nucleotide sequence encoding such muteins, to methods of determining in a subject a predisposition of having an age related disorder associated with PYCR1, to methods of identifying a compound capable of modifying the expression of PYCR1 and methods of treating a subject having an age-related disorder associated with PYCR1. The invention further relates to a genetically modified animal and a method of modifying the expression of the PYCR1 gene in an animal.Type: ApplicationFiled: May 26, 2010Publication date: June 7, 2012Applicant: Agency for Science, Technology and ResearchInventors: Bruno Reversade, Stefan Mundlos
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Patent number: 8178324Abstract: The present invention relates to a method for the deracemization or chiral inversion of chiral amines by enzymatic treatment. The method employs a stereoselective enzymatic conversion and either a non-selective or partially selective chemical or enzymatic conversion, simultaneously or sequentially. The invention also provides a method for selecting a suitable enzyme, particularly a suitable amine oxidase, and for the generation of novel enzymes suitable for use in the deracemization method.Type: GrantFiled: November 16, 2010Date of Patent: May 15, 2012Assignee: Ingenza LimitedInventors: Marina Victorovna Alexeeva, Alexis Enright, Mahmoud Mahmoudian, Nicholas Turner
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Patent number: 8168392Abstract: By finding a novel tetrahydrofolate synthetase gene and a protein encoded by said gene, a method for identifying a compound which inhibits cell growth accelerating activity of said protein is provided, and a judging method, a preventing method and a treating method of colon cancer are provided. A DNA comprising a nucleotide sequence of from the 94th to 2934th positions of the nucleotide sequence of SEQ ID NO:1 of the SEQUENCE LISTING; a polynucleotide which specifically hybridizes with said DNA; a protein encoded by said DNA; a recombinant vector comprising said DNA; a transformant comprising said recombinant vector; an antibody for said protein; a method for producing said protein; a method for identifying a compound which inhibits cell growth accelerating activity possessed by said protein; a method for judging colon cancer, characterizing in that expressed amount of said DNA is measured; a kit for judging colon cancer; a preventive agent and/or therapeutic agent for colon cancer.Type: GrantFiled: April 8, 2009Date of Patent: May 1, 2012Assignee: Daiichi Sankyo Co., Ltd.Inventor: Takeyuki Sugiura
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Publication number: 20120070870Abstract: The invention features methods and compositions relating to cells that have been engineered to reduce or eliminate proteins having enzymatic activity that interfere with the expression of a metabolic product.Type: ApplicationFiled: June 1, 2010Publication date: March 22, 2012Applicant: Ginkgo BioWorksInventors: Jeffrey C. Way, Joseph H. Davis
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Publication number: 20120070876Abstract: The present invention relates to genetically modified proteins with uricolytic activity. More specifically, the invention relates to proteins comprising truncated urate oxidases and methods for producing them, including PEGylated proteins comprising truncated urate oxidases.Type: ApplicationFiled: September 7, 2011Publication date: March 22, 2012Applicant: Savient Pharmaceuticals, Inc.Inventors: Jacob Hartman, Simona Mendelovitz
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Publication number: 20120045816Abstract: Provided herein are glycosylated polypeptide compositions with substantially reduced Neu5Gc content. The glycosylated polypeptides compositions with substantially reduced Neu5Gc content can be obtained from cell sources cultured with Neu5Gc competitor or from non-human animal sources fed a diet supplemented with Neu5Gc competitor. Also provided herein are methods of treating a human subject with said compositions.Type: ApplicationFiled: July 14, 2011Publication date: February 23, 2012Inventors: Darius Ghaderi, Ajit Varki
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Patent number: 8105800Abstract: Composition for accurately assaying a glycated protein by: 1) avoiding effects of globulin and ascorbic acid components, 2) siabilizing proteases and at least enzymes acting on glycated amino acids; 3) accurately assaying albumin; and 4) assaying glycated albumin while avoiding the effects of glycated hemoglobin, and an assay method are provided. Thus, the contents of a glycated protein and glycated albumin can be more accurately determined.Type: GrantFiled: July 31, 2007Date of Patent: January 31, 2012Assignee: Asahi Kasei Pharma CorporationInventors: Takuji Kouzuma, Issei Yoshioka, Motoo Arai, Junichi Sumitani, Shigeyuki Imamura
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Patent number: 8097460Abstract: The present invention relates to the production of ethanol as a product of bacterial fermentation. In particular this invention relates to a novel method of gene inactivation and gene expression based upon homologous recombination. The method is particularly useful in connection with species of Bacillus such as B. stereothermophilus, B. calvodelox, B. caldotenax, B. thermoglucosidasius, B. coagulans, B. licheniformis, B. thermodenitrificans, and B. caldolyticus.Type: GrantFiled: February 24, 2009Date of Patent: January 17, 2012Assignee: Elsworth Biotechnology LimitedInventors: Muhammed Javed, Fiona Cusdin, Paul Milner, Edward Green
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Publication number: 20120009640Abstract: The present disclosure provides methods useful for producing fatty alcohol compositions from recombinant host cells. The disclosure further provides variant fatty acyl-CoA reductase (FAR) enzymes, polynucleotides encoding the variant FAR enzymes, and vectors and host cells comprising the same.Type: ApplicationFiled: June 28, 2011Publication date: January 12, 2012Applicant: Codexis, Inc.Inventors: Behnaz Behrouzian, Louis Clark, Yihui Zhu, Michael Clay, Kristian Karlshoej
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Patent number: 8071340Abstract: A process for the production of ortho-aminophenolic analogs of chloramphenicol using a biocatalyst consisting of pure enzymes, partially purified enzymes, cell lysate, intact cells, or a metal reaction linked with a subsequent enzymatic reaction. The biocatalyst is an enzyme system that makes use of a nitroreductase enzyme that initially reduces the nitroarene to the hydroxylaminoarene and a mutase enzyme that converts the hydroxylaminoarene to an ortho-aminophenol. The biocatalyst can also consist of a coupled, two-step metal and enzyme reaction in which the metal, such as zinc, catalyzes the transformation of the nitroarene to the hydroxylaminoarene and the mutase then catalyzes the transformation of hydroxylaminoarene to the corresponding ortho-aminophenol.Type: GrantFiled: November 2, 2006Date of Patent: December 6, 2011Assignee: The United States of America as represented by the Secretary of the Air ForceInventors: Lloyd J. Nadeau, Heather R. Luckarift, Jim C. Spain
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Publication number: 20110295582Abstract: This invention provides for the design of novel nitrile oxidoreductases that can be used as biocatalysts for industrial chemical processes and; and thus, provide attractive alternatives to traditional chemical synthesis. Generally, this technology relates to crystal structures of nitrile oxidoreductases, and of crystal structures of nitrile oxidoreductases complexed with substrates and co-factors. For example, the invention provides for the crystalline structure of the nitrile oxidoreductase, QueF, as well as for a computer-readable medium having QueF crystal structure information stored thereon.Type: ApplicationFiled: December 30, 2010Publication date: December 1, 2011Inventors: Dirk IWATA-REUYL, Manal A. Swairjo
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Patent number: 8067553Abstract: A naturally occurring or recombinant urate oxidase (uricase) covalently coupled to poly(ethylene glycol) or poly(ethylene oxide) (both referred to as PEG), wherein an average of 2 to 10 strands of PEG are conjugated to each uricase subunit and the PEG has an average molecular weight between about 5 kDa and 100 kDa. The resulting PEG-uricase conjugates are substantially non-immunogenic and retain at least 75% of the uricolytic activity of the unmodified enzyme.Type: GrantFiled: April 28, 2010Date of Patent: November 29, 2011Assignees: Mountain View Pharmaceuticals, Inc., Duke UniversityInventors: L. David Williams, Michael S. Hershfield, Susan J. Kelly, Mark G. P. Saifer, Merry R. Sherman
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Publication number: 20110287494Abstract: Novel enzymes that stereoselectively reduce imine derivatives were isolated and purified, and polynucleotides encoding the enzymes were cloned. Optically active amine derivatives were produced by acting on imine derivatives with a culture of microorganisms having the ability to stereoselectively reduce the compounds, microbial cells or processed products thereof, and/or imine reductases thereof, followed by collecting the generated optically active amine derivatives. The present invention enables, for example, production of an optically active compound represented by formula (IV): (wherein R group represents an alkyl group having one to three carbon atoms; and n represents an integer of 1 to 4).Type: ApplicationFiled: September 1, 2009Publication date: November 24, 2011Applicant: Daicel Chemical Industries LtdInventors: Toru Nagasawa, Toyokazu Yoshida, Koichi Ishida, Hiroaki Yamamoto, Norihiro Kimoto
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Publication number: 20110281309Abstract: The present invention relates to a novel amino acid dehydrogenase, DNA encoding the enzyme, and a transformant having the DNA introduced therein. The present invention also relates to a process for producing an L-amino acid, 2-oxo acid or D-amino acid, which includes allowing the amino acid dehydrogenase or a microorganism or transformant capable of producing the enzyme to act on a substrate compound. The amino acid dehydrogenase has good reactivity even with an amino acid or a 2-oxo acid each having a bulky side chain such as an aromatic-ring-containing group, which acids are poorly reactive with conventional amino acid dehydrogenases. The amino acid dehydrogenase enables the inexpensive and highly efficient production of a useful optically active amino acid.Type: ApplicationFiled: December 8, 2009Publication date: November 17, 2011Applicant: KANEKA CORPORATIONInventors: Hiroyuki Kanamaru, Ryuuji Miki, Makoto Ueda, Hironori Nanba, Yoshihiko Yasohara
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Publication number: 20110268713Abstract: The present invention provides uricases and methods of their production and use in reducing the amount of uric acid in a subject. The present invention further provides methods employing a uricase of this invention in the treatment and/or prevention of hyperuricemia, gout, tumor lysis syndrome and/or hypertension in a subject.Type: ApplicationFiled: April 8, 2011Publication date: November 3, 2011Inventor: Eric A. Gaucher
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Publication number: 20110265197Abstract: The present invention provides methods of detecting cancer using biomarkers.Type: ApplicationFiled: July 16, 2009Publication date: October 27, 2011Applicant: Dana-Farber Cancer Institute, Inc.Inventors: Ronald Depinho, Zhihu Ding, Lynda Chin
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Publication number: 20110262977Abstract: Optically active amine derivatives are produced by acting on imine derivatives with a culture of microorganisms having the ability to stereoselectively reduce the compounds, microbial cells, or processed products thereof, followed by collecting the generated optically active amine derivatives. Optically active amine derivatives obtained in the present invention are useful as materials for pharmaceutical agents. The present invention enables, for example, production of an optically active compound represented by formula (IV): (wherein R group represents an alkyl group having one to three carbon atoms; and n represents an integer of 1 to 4).Type: ApplicationFiled: September 1, 2009Publication date: October 27, 2011Applicant: Daicel Chemical Industries, Ltd.Inventors: Toru Nagasawa, Toykazu Yoshida, Koichi Ishida, Hiroaki Yamamoto, Norihiro Kimoto
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Publication number: 20110262476Abstract: The present invention relates to the use of mutant glycoproteins from pathogenic bacteria lacking one or more phosphorylcholine and/or glycosylation post-translational modifications as immunogens. These post-translational modifications act as masking structures that elicit an immune response which does not confer protection on an infected individual. The removal or modification of these masking structures alters the protein such that it elicits a stronger immune response to the protein and/or the bacterial pathogen. Particular examples are pilin proteins and nitrite reductase glycoproteins of Neisseria bacteria.Type: ApplicationFiled: August 28, 2009Publication date: October 27, 2011Inventor: Michael Paul Jennings
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Patent number: 8026078Abstract: The present invention provides a method of measuring a glycated protein in a sample using a redox reaction, by which the glycated protein can be measured accurately with high sensitivity. In order to remove a glycated amino acid present in the sample other than the glycated protein, the glycated amino acid is degraded in advance by causing a fructosyl amino acid oxidase to act thereon, and thereafter, a fructosyl amino acid oxidase is caused to act on the glycated protein in the presence of a tetrazolium compound and sodium azide to cause a redox reaction. The amount of the glycated protein is determined by measuring the redox reaction. As the glycated protein, glycated hemoglobin is preferable.Type: GrantFiled: January 29, 2003Date of Patent: September 27, 2011Assignee: ARKRAY Inc.Inventors: Satoshi Yonehara, Kaori Ishimaru, Tsuguki Komori
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Publication number: 20110217755Abstract: The present invention relates to genetically modified proteins with uricolytic activity. More specifically, the invention relates to proteins comprising truncated urate oxidases and methods for producing them, including PEGylated proteins comprising truncated urate oxidases.Type: ApplicationFiled: May 13, 2011Publication date: September 8, 2011Applicant: Savient Pharmaceuticals, Inc.Inventors: Jacob Hartman, Simona Mendelovitz
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Publication number: 20110201053Abstract: Compositions and methods comprising recombinant expression vector elements (rEVEs) to enhance the level of expression of recombinant proteins are described. Other compositions and methods for lowering, substantially suppressing, or essentially silencing expression of a recombinant protein are also described.Type: ApplicationFiled: April 29, 2011Publication date: August 18, 2011Inventors: WENDY R. GION, GERALD R. CARSON, HONG GAO, YUNE Z. KUNES
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Publication number: 20110136202Abstract: Disclosed are: a eukaryotic amadoriase which is prepared by introducing a mutation into DNA encoding a eukaryotic amadoriase derived from a microorganism belonging to the genus Coniochaeta or Eupenicillium so as to introduce a substitution into a specific amino acid residue in the eukaryotic amadoriase, thereby overcoming the defect associated with thermal stability; a gene or recombinant DNA for the eukaryotic amadoriase; and a process for production of a eukaryotic amadoriase having excellent thermal stability.Type: ApplicationFiled: February 14, 2011Publication date: June 9, 2011Applicant: KIKKOMAN CORPORATIONInventors: Kozo HIROKAWA, Atsushi ICHIYANAGI
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Patent number: RE43795Abstract: The present invention provides a method of pretreating a sample containing a glycated amine as an analyte, thereby enabling highly reliable measurement of a glycated amine. A glycated amino acid in the sample is degraded by causing a fructosyl amino acid oxidase (FAOD) to act thereon, and thereafter, a FAOD further is caused to act on the glycated amine as the analyte in the sample to cause a redox reaction. The amount of the glycated amine is determined by measuring the redox reaction. The substrate specificity of the FAOD caused to act on the glycated amino acid may be either the same as or different from that of the FAOD caused to act on the glycated amine. When using the same FAOD, a FAOD is caused to act on the glycated amino acid to degrade it, and thereafter, the sample is treated with a protease to inactivate the FAOD and also to degrade the glycated amine.Type: GrantFiled: October 9, 2002Date of Patent: November 6, 2012Assignee: ARKRAY, Inc.Inventors: Satoshi Yonehara, Tsuguki Komori