Abstract: There is disclosed a variant-type carbohydrate hydrolase that has been increased transglycosylation activity by substituting another amino acid residue for the tyrosine residue that is present in the active center of the hydrolase, which hydrolase is an amylase or an enzyme analogous to amylase; a gene or a DNA sequence of the carbohydrate hydrolase with mutation introduced into the base sequence that encodes the tyrosine residue; and a vector or a transformant which comprises the DNA sequence. There is also disclosed a method for producing a variety of oligosaccharides and the like by using the variant-type carbohydrate hydrolase.
Type:
Grant
Filed:
June 6, 1995
Date of Patent:
May 20, 1997
Assignee:
Director-General Of Agency of Industrial Science and Technology
Abstract: The present invention relates to a cDNA probe for the detection of the mRNA for human methenyltetrahydrofolate synthetase, which comprises the nucleic acid sequence as shown in FIG. 6 or any functional analogs thereof wherein the hybridization of the probe and the mRNA for human methenyltetrahydrofolate synthetase is substantially preserved. The present invention also relates to a polyclonal antibody or an antigen-binding fragment thereof for the detection of the mRNA for human methenyltetrahydrofolate synthetase, wherein said antibody is raised against a protein segment aa.sup.100-112 H-Phe-Asp-Lys-His-Gly-Asn-Arg-Leu-Gly-Lys-OH of human methenyltetrahydrofolate synthetase.
Abstract: Method of isolating deletion mutants of Vibrio cholerae, wherein the deletion is predetermined by digestion with restriction endonucleases of known specificity. The deletions are inserted into the Vibrio cholerae chromosome by in vivo recombination between a plasmid carrying the desired deletion, with adjacent flanking sequences, and the Vibrio cholerae chromosome. The invention includes the isolation and characterization of a new Vibrio cholerae strain, CVD103Hg (ATTC No. 55,456), having a deletion in the tox gene, as defined by Acc I, Xba I, Cla I and/or restriction endonuclease sites, and carrying a mercury resistance gene. The invention also includes vaccines for protecting against the symptoms of cholera as well as methods for achieving this protection.
Abstract: A method of adjunctive therapy to inhibit reocclusions in a patient, e.g., after thrombolytic therapy or angioplasty, by administering to the patient a bolus of an amount of purified pro-urokinase ("pro-UK") that inhibits the formation of occlusive thrombi without inducing a systemic effect in the patient, the pro-UK is administered after the completion of the thrombolytic treatment and periodically thereafter for the duration of therapy, and becomes incorporated into the outer membrane of the platelets of the patient, thereby increasing the T.sub. 1/2 of the pro-UK in plasma, which is about 7 to 8 minutes, to about 4 to 5 days, and inhibiting reocclusion without inducing a systemic effect.
Abstract: The present invention is directed to nucleic acid sequences encoding Dendroides canadensis thermal hysteresis proteins. The THPs of Dendroides have significantly greater thermal hysteresis activity than any other known anti-freeze protein. The thermal hysteresis activity of the purified THPs can be further enhanced by combining the THPs with various "activating" compounds.
Abstract: The present invention provides an inexpensive fermentation medium for growing microorganisms. Also provided are fermentation media and methods for producing norleucine by growing E. coli thereon, fermentation media and methods for incorporating norleucine into polypeptides expressed by microorganisms grown thereon, and fermentation media and methods for preventing the incorporation of norleucine into polypeptides expressed by microorganisms grown thereon. Also provided are bovine somatotropin analogs.
Type:
Grant
Filed:
June 6, 1995
Date of Patent:
April 22, 1997
Assignee:
The Upjohn Company
Inventors:
David P. Brunner, Gary C. Harbour, Richard J. Kirschner, James F. Pinner, Robert L. Garlick
Abstract: A Bacillus cell contains a mutation in the epr gene resulting in inhibition of the production by the cell of the proteolytically active epr gene product; the cell may further contain mutations in the genes encoding proteolytically active residual protease I (RP-I) and proteolytically active residual protease II (RP-II).
Type:
Grant
Filed:
September 7, 1990
Date of Patent:
April 15, 1997
Assignee:
Omnigene, Inc.
Inventors:
Alan Sloma, Gerald A. Rufo, Jr., Cathy F. Rudolph, Barbara J. Sullivan, Janice Pero
Abstract: The present invention relates to a method for producing high levels of functional recombinant proteins in adenovirus-transformed mammalian cells by incubating cells capable of producing recombinant proteins at a temperature range between about 38 degrees centigrade and about 39 degrees centigrade. The method allows for higher levels of expression of total protein in some cell lines and higher levels of functional protein in other cell lines.
Abstract: Functional human factor VIII produced recombinantly is used in the treatment of human beings diagnosed to be deficient in factor VIII coagulant activity. Also provided are DNA isolates and expression vehicles encoding functional human factor VIII, as well as transformed host cells and processes for producing human factor VIII by use of recombinant DNA technology.
Type:
Grant
Filed:
February 3, 1992
Date of Patent:
April 8, 1997
Assignee:
Genentech, Inc.
Inventors:
Daniel J. Capon, Richard M. Lawn, Gordon A. Vehar, William I. Wood
Abstract: Functional human factor VIII produced recombinantly is used in the treatment of human beings diagnosed to be deficient in factor VIII coagulant activity. Also provided are DNA isolates and expression vehicles encoding functional human factor VIII, as well as transformed host cells and processes for producing human factor VIII by use of recombinant DNA technology.
Type:
Grant
Filed:
August 20, 1990
Date of Patent:
April 8, 1997
Assignee:
Genentech, Inc.
Inventors:
Daniel J. Capon, Richard M. Lawn, Gordon A. Vehar, William I. Wood
Abstract: Tissue plasminogen activator (t-PA) zymogens and variants are prepared, including a fibrinolytically active variant of t-PA that has an amino acid alteration at a site within the protease domain of t-PA as compared with the corresponding wild-type t-PA, which alteration renders the variant zymogenic in the presence of plasmin-degraded fibrinogen, and/or fibrin (or plasma clot) specific, as compared to the corresponding wild-type t-PA. DNA sequences can be prepared that encode the zymogens and variants, as well as expression vectors incorporating the DNA sequences, and host cells transformed with the expression vectors. The zymogens and variants may be used in a pharmaceutical preparation to treat a vascular disease or condition or to prevent fibrin deposition or adhesion formation or reformation in mammals.
Type:
Grant
Filed:
April 14, 1995
Date of Patent:
April 1, 1997
Assignee:
Genentech, Inc.
Inventors:
Stephen Anderson, William F. Bennett, David Botstein, Deborah L. Higgins, Nicholas F. Paoni, Mark J. Zoller
Abstract: The sequences of a pair of human proteins, trichohyalin and transglutaminase-3, in addition to the sequence of the mouse transglutaminase-3 protein, have been discovered. The enzyme transglutaminase-3 is used to cross-link the structural protein trichohyalin in order to form a gel.
Type:
Grant
Filed:
April 30, 1993
Date of Patent:
April 1, 1997
Assignee:
The United States of America as represented by the Department of Health & Human Services
Inventors:
Peter M. Steinert, In-Gyu Kim, Soo-Il Chung, Sang-chul Park
Abstract: Neurotransmission by excitatory amino acids (EAAs) such as glutamate is mediated via membrane-bound surface receptors. DNA coding for one family of these receptors, of the kainate binding type of EAA receptors, has now been isolated and the receptor protein characterized. Herein described are recombinant cell lines which produce the EAA receptor as a heterologous membrane-bound product. Also described are related aspects of the invention, which are of commercial significance. Included is use of the cell lines as a tool for discovery of compounds which modulate EAA receptor stimulation.
Type:
Grant
Filed:
April 3, 1995
Date of Patent:
April 1, 1997
Assignee:
Allelix Biopharmaceuticals Inc.
Inventors:
Rajender Kamboj, Stephen L. Nutt, Lee Shekter, Michael A. Wosnick
Abstract: Tissue plasminogen activator (t-PA) zymogens and variants are prepared, including a fibrinolytically active variant of t-PA that has an amino acid alteration at a site within the protease domain of t-PA as compared with the corresponding wild-type t-PA, which alteration renders the variant zymogenic in the presence of plasmin-degraded fibrinogen, and/or fibrin (or plasma clot) specific, as compared to the corresponding wild-type t-PA. DNA sequences can be prepared that encode the zymogens and variants, as well as expression vectors incorporating the DNA sequences, and host cells transformed with the expression vectors. The zymogens and variants may be used in a pharmaceutical preparation to treat a vascular disease or condition or to prevent fibrin deposition or adhesion formation or reformation in mammals.
Type:
Grant
Filed:
April 26, 1995
Date of Patent:
March 25, 1997
Assignee:
Genentech, Inc.
Inventors:
Stephen Anderson, William F. Bennett, David Botstein, Deborah L. Higgins, Nicholas F. Paoni, Mark J. Zoller
Abstract: Neurotransmission by excitatory amino acids (EAAs) such as glutamate is mediated via membrane-bound surface receptors. DNA coding for one family of these receptors, of the kainate binding type of EAA receptors, has now been isolated and the receptor protein characterized. Herein described are recombinant cell lines which produce the EAA receptor as a heterologous membrane-bound product. Also described are related aspects of the invention, which are of commercial significance. Included is use of the cell lines as a tool for discovery of compounds which modulate EAA receptor stimulation.
Type:
Grant
Filed:
February 28, 1994
Date of Patent:
March 25, 1997
Assignee:
Allelix Biopharmaceuticals Inc.
Inventors:
Rajender Kamboj, Stephen L. Nutt, Lee Shekter, Michael A. Wosnick
Abstract: The present invention provides a novel ascorbate oxidase (ASOD) which catalyzes oxidation reaction of L-ascorbic acid with molecular oxygen to form L-dehydroascorbic acid and hydrogen peroxide, a process for producing the ascorbate oxidase comprising using a microorganism belonging to the genus Eupenicillium, a gene encoding ASOD, a transformant containing such a gene, a process for producing ASOD using such a transformant, and a reagent composition comprising ASOD, such as a reagent composition for examination, a food additive, and a reagent composition in the fields of food and clinical examination. The ascorbate oxidase has excellent stability particularly in a liquid state.
Abstract: The invention concerns tissue plasminogen activator (t-PA) variants which are glycosylated at any of positions 103-105, and are devoid of functional carbohydrate structure at position 117 of wild-type human t-PA amino acid sequence. The variants have extended circulatory half-life and substantially retained fibrin binding, or improved in vivo fibrinolytic potency, as compared to wild-type human t-PA.
Type:
Grant
Filed:
May 8, 1995
Date of Patent:
March 18, 1997
Assignee:
Genentech, Inc.
Inventors:
William F. Bennett, Bruce A. Keyt, Nicholas F. Paoni
Abstract: A method of producing a recombinant serine protease inhibitor capable of effectively modulating serine protease activity is provided. Compositions capable of modulating serine protease activity and use of such compositions to regulate inflammatory processes in cells are also provided.
Type:
Grant
Filed:
July 19, 1994
Date of Patent:
March 18, 1997
Assignee:
Trustees of the University of Pennsylvania
Inventors:
Harvey Rubin, Barry Cooperman, Norman Schechter, Michael Plotnick, Zhi M. Wang
Abstract: A coagulation active complex of Factor VIII fragments is produced by causing coagulation inactive FVIII heavy chain to react with coagulation inactive FVIII light chain in the presence of a complex forming agent. Thus, FVIII-HC and FVIII-LC are converted to coagulation active FVIII complex in the presence of divalent metal ions, such as Mn.sup.2+, Ca.sup.2+ or C.sup.2+, or a component of the pro-thrombin complex.