Abstract: A process is disclosed for continuously treating a solubilized protein solution containing a protein unfolded to some degree, in a small volume continuous flow reactor, to obtain the protein in a conformation exhibiting the protein's characteristic biological activity by continuously diluting out the solubilizing agent, while continuously withdrawing the refolded protein. The continuous process may be carried out using deionized water as a diluent, rather than buffer solutions.
Abstract: A method for recovering a recombinant protein from a protein solution containing high molecular weight contaminating proteins by directly adding a flocculant to the solution in amounts sufficient to selectively precipitate the high molecular weight protein contaminants is disclosed.The high molecular weight precipitates are removed and the solution is further processed to remove low molecular weight contaminating proteins and other non-protein contaminants. The recombinant protein is subsequently recovered and further processed to produce a protein composition suitable for its intended use.
Abstract: A protein characterized by the fact that it is a non-keratinic protein present on the apicolateral surface and absent on the basal surface of basal epidermal cells, in particular in man, that it is present in a nonpolarized manner in basocellular and spinocellular carcinomas and absent in melanoma and naevus cells; antibodies directed against said protein, their preparation and their use as reagents; cellular stocks secreting such antibodies, and their preparation.
Abstract: From a cDNA library, a nucleotide sequence of a novel gene, called rig, specifically expressed by streptozotocin- or alloxan-nicotinamide-induced rat insulinomas was determined and an amino acid sequence of a protein encoded by the gene was deduced. Further, novel genes with base sequences homologous to rig were found in a BK virus-induced hamster insulinoma and in a surgically removed human insulinoma. The above DNA is transcribed to provide an mRNA. The above novel proteins, DNAs and mRNAs can be efficaciously employed for the medical purposes of pancreatic diseases.
Abstract: The protein doublet H110D, the individual components thereof, and the production and use thereof in a vaccine against a nematode infection. This protein doublet is a plasma membrane-associated protein material of the intestinal microvilli of Haemonchus contortus. H110D has a molecular weight of about 110 kd and reacts with antibodies raised in animals injected with a contortin-enriched fraction. Injection of preparations of the protein doublet H110D or its components induces the production of specific protective antibodies.
Abstract: Peptides having essentially the sequence of bovine pancreatic trypsin inhibitor (aprotinin) wherein one or more of the amino acids at positions 15, 16, 17, 18, 34, 39 and 52 are replaced by any naturally occurring amino acid produced by recombinant DNA technology, process, expression vector and recominant host therefor and pharmaceutical use thereof. Such peptides being useful as therapeutic agents in diseases connected with the presence of excessive amounts of proteinases.
Type:
Grant
Filed:
July 20, 1988
Date of Patent:
June 2, 1992
Assignee:
Bayer Aktiengesellschaft
Inventors:
Ernst-August Auerswald, Wolfgang Bruns, Dietrich Horlein, Gerd Reinhardt, Eugen Schnabel, Werner Schroder
Abstract: To provide a new catenin concerning with the function of cell-cell adhesion, a gene encoding said catenin, and a use of said gene.Isolated neural .alpha.-catenin. A gene encoding neural .alpha.-catenin. A method of producing neural .alpha.-catenin by the method of genetic engineering. A method of controlling the function of cell-cell adhesion by using said gene. Antibodies capable of recognizing neural .alpha.-catenin. Amino acid sequense of said neural .alpha.-catenin and nucleotide sequence of said gene are also determined.
Abstract: The phosphorylated structural protein of molecular weight about 150 kd (pp 150) of human cytomegalovirus (HCMV) is highly immunogenic and is reliably recognised by human antisera. This protein can, after assignment and sequencing of the gene, be prepared, in whole or in immunogenic sections, by gene manipulation. Proteins of this type are suitable as reagents, for example in an ELISA, and as constituents of vaccines.
Type:
Grant
Filed:
April 28, 1995
Date of Patent:
December 8, 1998
Assignee:
Behring Diagnositcs GmbH
Inventors:
Gerhard Jahn, Birgit-Christine Scholl, Michael Broker, Michael Mach, Bernhard Fleckenstein, Bernd Traupe
Abstract: The present invention provides a glycoprotein derived from human cell membrane, which has a molecular weight of 20 to 25 Kd as estimated by SDS polyacrylamide gel electrophoresis, and contains N-glycoside type carbohydrate chain and phosphatidylinositol, and possesses an inhibitory activity to complement-mediated cell membrane damage. The present invention further provides a gene coding for the glycoprotein, and a method for the production of the glycoprotein and the gene therefor.
Abstract: Affinity-purified protein A preparations are contacted with a suitable anionic exchange material in order to remove trace contamination. Staphylococcal enterotoxin B (SEB) and other proteinaceous contaminants are removed by passing such affinity-purified protein A preparations through a DEAE-cellulose column and thereafter selectively eluting the protein A to separate the contaminants. Very high purity protein A composition are thus obtained, typically having a contaminant concentration of about 5 weight % or below, with below about 0.001 weight % SEB.
Abstract: The present invention discloses a new method for solubilizing and refolding recombinant proteins expressed as granules. The method involves sulfitolysis and the formation of a precipitate of protein-S-sulfonate by warming. The precipitate has been found to contain protein in high purity. In addition, proper folding takes place if the desired protein is fully reduced and passed through an intermediate concentration of denaturant which allows for a transition between its folded and unfolded states.
Abstract: A method of isolating cell surface receptors utilizing a short peptide sequence bound to an affinity column. Cell surface receptors which bind selectively to the short peptide and which are specific to various adhesion proteins may be isolated therewith from various cell preparations. These receptors, whose functional integrity has been maintained by the presence of the peptide ligand, are incorporated into liposomes and used to deliver specific compounds inside the liposomes to select tissues containing the specific adhesion proteins.
Type:
Grant
Filed:
July 13, 1990
Date of Patent:
April 27, 1993
Assignee:
La Jolla Cancer Research Foundation
Inventors:
Erkki I. Ruoslahti, Michael D. Pierschbacher
Abstract: The invention concerns a process for purifying protein A preparations to high purity with high product yield. Where the protein A is obtained from a Gram-negative recombinant microbe hosting a vehicle containing a gene encoding protein A, the protein A is purified to high purity, and, advantageously, to very low levels of endotoxin. The protein A preparations made via the invention process are useful in therapeutic application, e.g., therapeutic plasma exchange, as well as for other well-known uses of protein A.
Abstract: A method for recovering a recombinant protein from a protein solution containing high molecular weight containing proteins by directly adding amine or quaternary ammonium compounds to the solution in amounts sufficient to selectively precipitate the high molecular weight protein contaminants.The high molecular weight precipitates are removed and the solution is further processed to remove low molecular weight contaminating proteins and other non-protein contaminants. The recombinant protein is subsequently recovered and further processed to produce a protein composition suitable for its intended use.
Abstract: A method for recovering a recombinant protein from a protein solution containing high molecular weight contaminating proteins by directly adding Group IIA metal salts to the solution in amounts sufficient to selectively precipitate the high molecular weight protein contaminants is disclosed.The high molecular weight precipitates are removed and the solution is further processed to remove low molecular weight contaminating proteins and other non-protein contaminants. The recombinant protein is subsequently recovered and further processed to produce a protein composition suitable for its intended use.
Abstract: A fused protein comprising a polypetide containing an antibody binding site of protein A and a polypeptide of lymphotoxin, and having biological activities of lymphotoxin and an ability to bind to an antibody is disclosed. Further, a process for the production of the fused protein, as well as a DNA coding for the fused protein, a plasmid containing the DNA, and E. coli transformed with the plasmid, necessary for the above-mentioned process, are provided.
Type:
Grant
Filed:
January 24, 1989
Date of Patent:
March 10, 1992
Assignees:
Sagami Chemical Research Center, Central Glass Company, Ltd., Hodogaya Chemical Co., Ltd., Nippon Soda Company, Ltd., Nissan Chemical Industries, Ltd., Tosoh Corporation
Inventors:
Tetsuzo Miki, Seishi Kato, Hiroshi Osada
Abstract: A protein, in particular MAP 30, obtainable from both the fruit and seeds of Momordica charantia or produced by recombinant means useful for treating tumors and HIV infections is disclosed. In treating HIV infections, the protein is administered alone or in conjunction with conventional AIDS therapies. Also provided are processes for purifying the protein, DNA sequences encoding the protein, and recombinant DNA methods for expressing the protein.
Type:
Grant
Filed:
July 21, 1994
Date of Patent:
January 16, 1996
Assignees:
New York University, American Biosciences, Inc., The United States of America as represented by the Secretary of the Department of Health and Human Services
Inventors:
Sylvia Lee-Huang, Philip L. Huang, Peter L. Nara, Hao-Chia Chen, Hsiang-fu Kung, Peter Huang, Henry I. Huang, Paul L. Huang
Abstract: The present invention provides for a new polypeptide and a method for producing the same. The polypeptide has a molecular weight of approximately 30,000 daltons as a dimer and a monomer molecular weight of about 15,000 daltons, an isoelectric pH of about 4.47 and an activity of at least 21,000 units per milligram of protein in the monomer or dimer state. The preferred method comprises chromatographing a crude polypeptide-containing medium on a dextran derived chromatography column; precipitating the eluate in a water-ethanol solution; electrophoresing the precipitate in a polyacrylamide gel; and chromatographing the extract on a reverse phase-high performance liquid chromatography column.
Type:
Grant
Filed:
July 5, 1988
Date of Patent:
July 7, 1992
Assignee:
The University of Tennessee Research Corporation
Abstract: The present invention comprises a method for the purification of the 69 kDa outer membrane protein of Bordetella B. pertussis and the protein purified therewith. A preferred embodiment comprises the purification of the 69 kDa protein from Bordetella B. pertussis strain Bp 353. The present process is advantageous in that it does not require or involve the use of biologics (such as monoclonal antibodies) and therefore simplifies the purification procedure and makes the resulting purified protein particularly advantageous for inclusion in acellular vaccines.
Type:
Grant
Filed:
February 10, 1989
Date of Patent:
March 31, 1992
Assignee:
United States of America
Inventors:
Drusilla L. Burns, Michael J. Brennan, Jeanine L. Gould-Kostka, Charles R. Manclark
Abstract: A method for recovering a recombinant protein from a protein solution containing high molecular weight contaminating proteins by directly adding Group IIA metal salts to the solution in amounts sufficient to selectively precipitate the high molecular weight protein contaminants is disclosed.The high molecular weight precipitates are removed and the solution is further processed to remove low molecular weight contaminating proteins and other non-protein contaminants. The recombinant protein is subsequently recovered and further processed to produce a protein composition suitable for its intended use.