Search Patents
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Patent number: 5728553Abstract: A process for the preparation of albumin which has extremely low levels of or is essentially free of colorants, metal ions, human proteins, fragments of albumin, polymers or aggregates of albumin, and viruses, and which is relatively non-glycated, relatively high in free thiol and with an intact C-terminus. The process comprises passing albumin (preferably expressed and secreted by transformed yeast) through two chromatography purifications, ultrafiltering the product, passing through two further chromatography steps and again ultrafiltering the product.Type: GrantFiled: May 25, 1995Date of Patent: March 17, 1998Assignee: Delta Biotechnology LimitedInventors: Andrew R. Goodey, Darrell Sleep, Hendrik van Urk, Stephen Berezenko, John R. Woodrow, Richard A. Johnson, Patricia C. Wood, Steven J. Burton, Alan V. Quirk, David St. J. Coghlan, Mark J. Wilson
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Patent number: 4981951Abstract: A method of purifying a recombinant protein from a solution, such as tissue culture fluid, containing gylcoproteins. The affinity of lectins for specific glycoproteins is assessed and used to select a particular lectin specific for the contaminating glycoprotein(s). A sugar buffer such as alpha methyl mannoside prevents binding of the recombinant protein. The preferred lectin is lentil lectin, for use in separating recombinant Factor VIII from tissue culture fluid contaminated with rodent protein from the cell line used to produce the recombinant Factor VIII.Type: GrantFiled: April 14, 1988Date of Patent: January 1, 1991Assignee: Miles Inc.Inventor: Grace C. Tsay
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Patent number: 5179196Abstract: The present invention provides a process for the recovery of heterologous proteins from CTAP-III fusion proteins comprising expressing a fusion protein having a first amino acid sequence, a second amino acid sequence, and a selectable site which may be cleaved to provide first and second polypeptide fragments, respectively, wherein the first amino acid fragment is homologous to CTAP-III, and the first and second fragments have different pI values; cleaving the fusion protein to provide the first and second fragments; and separating the first and second fragments by ion exchange chromatography.Type: GrantFiled: May 4, 1989Date of Patent: January 12, 1993Assignee: SRI InternationalInventors: Paul H. Johnson, Ping Sze, Richard C. Winant, Jerome B. Lazar
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Patent number: 5004806Abstract: The present invention encompasses a method for removing proteins from a solution containing polynucleotides and proteins comprising filtering the solution through a nitrocellulose membrane at neutral or basic pH.Type: GrantFiled: October 17, 1988Date of Patent: April 2, 1991Assignee: Molecular Devices CorporationInventor: Viola T. Kung
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Patent number: 4985544Abstract: Reactivation of cysteine-containing protein in a process, in which a reduced and denatured cysteine-containing protein such as salmon growth hormone I or eel growth hormone I can be efficiently reactivated.Type: GrantFiled: August 2, 1988Date of Patent: January 15, 1991Assignee: Kyowa Hakko Kogyo Co., Ltd.Inventors: Yoshiharu Yokoo, Seiji Sugimoto
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Patent number: 5066786Abstract: A method is described for the purification of crude human interferon from solutions containing it, which comprises:a) the complete adsorption of the crude interferon in a column of siliceous material which has previously been disinfected with an aqueous solution of formaldehyde;b) the washing of the column with non-pyrogenic, sterile, deionized water;c) the removal of the extraneous residual proteins by the elution of the column successively with a 1.4 M aqueous solution of NaCl in non-pyrogenic, sterile, deionized water, and with an aqueous solution of acetic acid having a molar concentration of 0.001 M to 0.003 M;d) the elution of the interferon from the column with an aqueous solution of acetic acid having a molar concentration of from 0.01 to 0.03 M and finally,e) the recovery and lyophilization of the elution containing the purified interferon.Type: GrantFiled: July 18, 1988Date of Patent: November 19, 1991Assignee: Sclavo, S.p.A.Inventors: Otello Protasi, Paolo Rappuoli
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Patent number: 5116952Abstract: Substantially pure proteins active in humoral hypercalcemia of malignancy (PTHrP) and sub-units and fragments thereof. Antibody reagents capable of binding to epitopes of PTHrP. Methods and kits for the detection of PTHrP.Type: GrantFiled: May 9, 1988Date of Patent: May 26, 1992Assignee: The University of MelbourneInventors: Thomas J. Martin, Jane M. Moseley, Bruce E. Kemp, Richard E. H. Wettenhall
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Patent number: 5095092Abstract: The invention relates to a process for the isolation and purification of hirudin from complex and salt-containing solutions by hydrophobic chromatography, using as stationary phase porous adsorber resins and as mobile phase organic solvents which are miscible with water.Type: GrantFiled: September 27, 1990Date of Patent: March 10, 1992Assignee: Hoechst AktiengesellschaftInventors: Werner Badziong, Peter Crause, Paul Habermann, Dominique Tripier
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Patent number: 5008377Abstract: A method for the preparation of a protein in a physiologically active or native form, which method includesproviding a source of protein in a solubilized form,and a cationic exchange medium;contacting the source of protein and cationic exchange medium; andrecovering the protein in a physiologically active form.Type: GrantFiled: April 21, 1988Date of Patent: April 16, 1991Assignee: Bunge (Australia) Pty. Ltd.Inventors: Joseph J. Patroni, Malcolm R. Brandon
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Patent number: 5077390Abstract: A substantially pure, hemagglutinin-free composition of trichosanthin, and a method of producing the composition is disclosed. A plant extract from Trichosanthes kirilowii is contacted with an anionic exchange resin to remove contaminating hemagglutinins, and trichosanthin is further purified from the extract by cation exchange chromatography to a purity of greater than 95%.Type: GrantFiled: September 7, 1989Date of Patent: December 31, 1991Assignee: Genelabs, IncorporatedInventors: Paul S. Wu, Susan B. Wade, Raul R. Soikes
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Patent number: 4983722Abstract: Protein A is selectively isolated from an antibody--Protein A mixture by exposing the mixture to an anion exchange material under conditions sufficient to adsorb both components and then sequentially eluting the antibodies and protein A under conditions of increasing ionic strength. Resulting antibody preparations have less than about 15 ng of Protein A per mg of antibody.Type: GrantFiled: June 8, 1988Date of Patent: January 8, 1991Assignee: Miles Inc.Inventors: James W. Bloom, Melvin F. Wong, Gautam Mitra
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Patent number: 4992531Abstract: A method for the recovery of proteins in a solubilized form from host cells including providing a source of host cells incorporating a synthesized or expressed protein; providing a source of at least one cationic surfactant; and treating the host cells with at least one cationic surfactant, in an amount sufficient to effect solubilization of the proteins.Type: GrantFiled: June 13, 1988Date of Patent: February 12, 1991Assignee: Bunge (Australia) Pty. Ltd.Inventors: Joseph J. Patroni, Malcolm R. Brandon
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Patent number: 4981952Abstract: The recovery of vitamin K-dependent proteins produced by transformed microorganisms can be effected from the cell culture medium utilizing the changes in the protein which occur in the presence of divalent cations. The present process uses divalent cations to alter the binding affinity of the proteins and thereby selectively elute the proteins away from contaminants in the culture medium using standard chromatography.Type: GrantFiled: August 16, 1989Date of Patent: January 1, 1991Assignee: Eli Lilly and CompanyInventor: S. Betty Yan
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Patent number: 5314993Abstract: 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.Type: GrantFiled: February 10, 1992Date of Patent: May 24, 1994Assignee: Repligen CorporationInventors: Richard N. Love, Albert T. Profy
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Patent number: 5415859Abstract: 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.Type: GrantFiled: August 14, 1992Date of Patent: May 16, 1995Inventor: Edward A. Munn
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Patent number: 5101014Abstract: 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: GrantFiled: February 10, 1989Date of Patent: March 31, 1992Assignee: United States of AmericaInventors: Drusilla L. Burns, Michael J. Brennan, Jeanine L. Gould-Kostka, Charles R. Manclark
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Patent number: 5169936Abstract: A process for the purification of proteins from solutions containing contaminants of similar net charge and molecular weight is provided, comprising contacting a solution containing the desired protein with an immobilized metal affinity chromatography resin in a buffer containing a low concentration of a weak ligand for the chelant of the resin. The adsorbed protein is then eluted using a buffer having a high concentration of the same weak ligand, e.g., Tris. Particularly preferred features employ agarose-iminodiacetic acid resins having copper cations and are especially useful in obtaining preparations of homogeneous, stable rsT4 proteins.Type: GrantFiled: April 14, 1989Date of Patent: December 8, 1992Assignee: Biogen, Inc.Inventors: Mark A. Staples, Christopher A. Pargellis
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Patent number: 5242812Abstract: Processes are provided for producing purified, hepatitis B surface antigen particles in mammalian cells which comprise culturing mammalian cells which produce the particles in a culture medium supplemented with a serum free of high molecular weight contaminant proteins and recovering the purified, hepatitis B surface antigen particles.Removal of molecules having a molecular weight greater than about 3.times.10.sup.5 daltons by prefractionation, for example, allows cells to be grown in culture media containing high levels of fetal calf serum, removes high molecular weight contaminant proteins which may be inhibitory to cell growth and simplifies purification of HBsAg since high molecular weight contaminant proteins are the major contaminants removed by purification processes.Type: GrantFiled: November 12, 1991Date of Patent: September 7, 1993Assignee: Bio-Technology General Corp.Inventor: Zeev Even-Chen
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Patent number: 4965344Abstract: A process for the preparation of a spatial form, which has biological activity, of a protein from a biologically inactive spatial form is described and comprises the protein being dissolved with the addition of a denaturing agent and thus converted into the random coil form, and the solution being allowed to pass through a material which has molecular sieve properties and contains a liquid medium in which the protein can assume a spatial form which has biological activity, and this material having molecular sieve properties being selected so that the molecules of the denaturing agent can penetrate, but the protein molecules canot. It is possible by centrifugation, blowing or sucking out to remove the medium in the "external volume" of the molecular sieve and to increase the rate of passage of the solution through the molecular sieve.Type: GrantFiled: June 2, 1987Date of Patent: October 23, 1990Assignee: Behringwerke AktiengesellschaftInventor: Reinhard Hermann
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Patent number: 5112951Abstract: The present invention provides a method for the separation of anti-metal chelate antibodies from non-specific proteins, including antibodies, by applying a preparation containing the anti-metal chelate antibodies to an oxo acid derivatized solid support and eluting first with an elution buffer containing sufficient salt concentration to elute non-specific proteins but not sufficient to elute the anti-metal chelate antibodies and then increasing the salt concentration of the elution solution so as to elute the anti-metal chelate antibodies. In one embodiment, the oxo acid derivatized solid support is a sulfopropyl resin. Appropriate salts include sodium phosphate, sodium chloride and sodium acetate. The method can be used to separate monoclonal or polyclonal anti-metal chelate antibodies from non-specific proteins as well as to separate bifunctional anti-metal chelate antibodies from monoclonal anti-metal chelate antibodies and other non-specific proteins.Type: GrantFiled: July 31, 1989Date of Patent: May 12, 1992Assignee: Hybritech IncorporatedInventors: Daniel E. Beidler, Rodney A. Jue