With Added Material Patents (Class 530/419)
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Patent number: 6936414Abstract: Provided herein is a method for separating nucleic acid from a test sample comprising the steps of contacting a test sample with a metal oxide support material and a binding buffer to form nucleic acid/metal oxide support material complexes, separating the complexes from the test sample; and eluting the nucleic acid from the metal oxide support material.Type: GrantFiled: December 22, 1999Date of Patent: August 30, 2005Assignee: Abbott LaboratoriesInventor: Gerard Gundling
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Patent number: 6927282Abstract: Protein suspensions comprising soluble and insoluble components are purified via flocculation with anionic polymers, such as polyacrylamides, potato starch, or modified cellulose. The procedure improves the efficiency of solid/liquid separations and can minimize or eliminate the requirement for centrifugation and/or filtration in large scale biotechnological processes. The method is particularly well suited for the purification and clarification of protein suspensions containing soluble somatotropin monomer using polyacrylamide and polysaccharide flocculants.Type: GrantFiled: August 27, 2001Date of Patent: August 9, 2005Assignees: Monsanto Technology LLC, Cytec Technology Corp.Inventors: Mark L. Chivers, Algird S. Cibulskas
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Patent number: 6900034Abstract: The invention relates to a method for solubilising and purifying recombinant proteins which are expressed in bacterial host cells and are deposited as insoluble aggregates (inclusion bodies). The purification is based on conversion of the inclusion bodies into soluble forms using organic denaturing reagents and using chromatographic methods. Inorganic, alkaline, salt-containing eluents are selected here which, after purification is complete, enable the recombinant proteins, after neutralisation, to be made available in a form which can be employed directly for medical use and is physiologically acceptable. The method is particularly suitable for purifying allergens and allergen fragments.Type: GrantFiled: August 18, 2001Date of Patent: May 31, 2005Assignee: Merck Patent GmbHInventors: Roland Suck, Oliver Cromwell, Helmug Fiebig
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Patent number: 6893639Abstract: The method for immune serum globulin purification relates to the purification of immune globulins from blood plasma with a high degree of efficiency and a high rate of recovery. The immune globulin source is Cohn's fraction I+II+III or II+III prepared from plasma or plasma intermediates by precipitation of the paste at pH 5.7 to 5.8 in the presence of 20% ethanol and 80% purified water. A glycine extraction is followed by an anion exchange chromatography column step to achieve a significantly high yield and high purity of the concentrated protein.Type: GrantFiled: October 19, 2001Date of Patent: May 17, 2005Assignee: Hemacare CorporationInventors: Joshua Levy, Fred Rothstein, Bahman Shimiaei
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Patent number: 6875848Abstract: The gammaglobulin is extracted from a fraction isolated by fractionation with ethanol in the presence of a carbohydrate, and after reducing the content of contaminants with PEG, it is applied to an anionic resin exchange column, an effluent being obtained in which the PEG content is subsequently reduced by ultrafiltration and which is concentrated in order to carry out sequentially an optional treatment at an acid pH and at least one of the following steps of viral inactivation, consisting of pasteurisation and a treatment with solvent/detergent, the product afterwards being precipitated and washed with PEG in order to eliminate any chemical viral inactivation reagents and then, by solubilisation and change of pH, the protein contaminants, and finally purified by ultrafiltration to reduce the volume and the PEG content, then carrying out an optional virus filtration and subsequent concentration.Type: GrantFiled: January 17, 2002Date of Patent: April 5, 2005Assignee: Probitas Pharma, S.A.Inventors: Pere Ristol Debart, Francisco Rabaneda Gimenez, Ma Teresa Lopez Hernandez
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Patent number: 6875617Abstract: A method of protein precipitation, concentration and removal of non-protein agents from the protein solution wherein the protein solution is treated with a protein-precipitation agent containing an acidic agent, a salt and a precipitate forming agent. After precipitation, the protein precipitate is washed with a water miscible organic solvent agent to remove non-protein agents present in the protein precipitate.Type: GrantFiled: April 27, 2001Date of Patent: April 5, 2005Assignee: Geno Technology, Inc.Inventor: Aftab Alam
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Patent number: 6852833Abstract: The present invention provides an artificial chaperon useful for refolding the proteins having low voluntary folding ability and being difficult or unable to be a native form without a second (or assistant) of a molecular chaperon in a short time, and folding said proteins as an active form. The present invention relates to an artificial chaperon kit characterized in that the kit comprises cyclic saccharide cycloamylose and polyoxyethylenic detergent or cyclic saccharide cycloamylose and ionic detergent. The present invention also relates to a method for diluting the denaturant making the protein a denatured state by adding a specific detergent to a denatured protein, and preventing protein molecules from aggregation, thereafter adding cyclic saccharide cycloamylose, utilizing the inclusion ability thereof to strip detergent, accelerating the proper folding of protein into a correct higher-order structure with activity.Type: GrantFiled: August 10, 2000Date of Patent: February 8, 2005Assignees: Director of National Food Research Institute, Ministry of Agriculture, Forestry and Fisheries, Bio-oriented Technology Research Advancement InstitutionInventors: Sachiko Machida, Kiyoshi Hayashi
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Patent number: 6756482Abstract: The present invention provides a process for purifying human activin by cation exchange chromatography and chaotropic ion concentration gradient elution.Type: GrantFiled: November 27, 2000Date of Patent: June 29, 2004Assignee: Ajinomoto Co., Inc.Inventors: Kunio Ono, Shigekatsu Tsuchiya, Daisuke Ejima, Yuzuru Eto
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Patent number: 6737233Abstract: A 24 kd percent capable of binding the E2 envelope protein of hepatitis C virus (HCV), and functionally equivalent variants or fragments of the 24 kd protein, are disclosed. Processes for production and purication of the 24 kd protein, and functionally equivalent variants or fragments thereof, are also disclosed.Type: GrantFiled: February 17, 1998Date of Patent: May 18, 2004Assignee: Chiron S.r.l.Inventor: Sergio Abrignani
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Publication number: 20040033224Abstract: Methods for producing biological solutions such as immunoglobulins and in particular anti-D immunoglobulin substantially free of abnormal prion protein resulting therefrom. Specifically provided are methods for aggregation of prions and depth filtration of the biological solution to capture and remove abnormal and if desired, normal prion protein. The prion protein may then be eluted from the depth filter and filter washes and concentrated sufficient for detection at limits currently required by available assays.Type: ApplicationFiled: May 23, 2003Publication date: February 19, 2004Inventors: Robert W. Van Holten, Stephen M. Autenrieth
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Publication number: 20040014084Abstract: Provided is a method of isolating a bio-molecule from a water-borne mixture, the method comprising: contacting the water-borne mixture with dimethyl ether to form solid particles of the bio-molecule.Type: ApplicationFiled: February 25, 2003Publication date: January 22, 2004Applicant: Phasex CorporationInventors: Val Krukonis, Kara T. Williams, Anthony Gudinas, Hans Schonemann, Paula Wetmore
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Non-aqueous injectable formulation preparation with pH adjusted for extended release of somatotropin
Patent number: 6664234Abstract: The present invention provides compositions of matter which allow for the extended release and enhanced bioavailability of biologically-active polypeptides following parenteral delivery to an animal. More particularly, it concerns compositions comprising biologically-active somatotropin formulated for extended release, methods of preparing these compositions, and methods of using the same. These compositions comprise somatotropin, a pH-adjusting constituent (PAC), and a substantially non-aqueous, hydrophobic excipient. The PAC may comprise any suitable, biocompatible compound including, but not limited to one or mixtures of two or more of the following: acetic acid, phosphoric acid, monobasic phosphate. The PAC is added to the compositions of matter in an amount effective to adjust the pH to or near to the isoelectric point (pI) of the somatotropin component.Type: GrantFiled: June 28, 2001Date of Patent: December 16, 2003Assignee: Monsanto Technology LLCInventors: Daniel N. Heintz, Yunhua N. Jeng -
Publication number: 20030208052Abstract: A sample is prepared from blood in a manner which makes it possible to further analyze proteins in the sample, e.g. to detect prions in the sample. Blood is extracted, allowed to clot and subjected to separation processing (e.g. centrifugation) to obtain serum. The serum is treated with a complexing agent which agent binds prions in the sample forming an agent/protein complex which makes it possible to concentrate the complex. Concentration of the complex results in a sample which can be successfully analyzed, e.g. assayed using a range of different types of assay methodologies for detecting prions.Type: ApplicationFiled: April 28, 2003Publication date: November 6, 2003Applicant: The Regents of the University of CaliforniaInventors: Stanley B. Prusiner, Jiri G. Safar
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Patent number: 6635746Abstract: Immunogenic compositions including vaccines are described that comprise an outer membrane antigen extract of a strain of Chlamydia and are effective in protection against disease caused by Chlamydia infection The immunogenic compositions may comprise the major outer membrane protein (MOMP) of Chlamydia which may be in a homooligomeric form or complexed with at least one other antigen of Chlamydia. The immunogenic composition may include an immunostimulating complex (ISCOM) and the outer membrane antigen may be incorporated therein. The immunogenic compositions have utility as chlamydial vaccines and in diagnostic applications.Type: GrantFiled: May 28, 1999Date of Patent: October 21, 2003Assignee: Aventis Pasteur LimitedInventors: Andrew D. Murdin, Brian J. Underdown
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Publication number: 20030170815Abstract: The invention relates to a method for solubilising and purifying recombinant proteins which are expressed in bacterial host cells and are deposited as insoluble aggregates (inclusion bodies). The purification is based on conversion of the inclusion bodies into soluble forms using organic denaturing reagents and using chromatographic methods. Inorganic, alkaline, salt-containing eluents are selected here which, after purification is complete, enable the recombinant proteins, after neutralisation, to be made available in a form which can be employed directly for medical use and is physiologically acceptable. The method is particularly suitable for purifying allergens and allergen fragments.Type: ApplicationFiled: March 7, 2003Publication date: September 11, 2003Inventors: Roland Suck, Oliver Cromwell, Helmug Fiebig
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Patent number: 6613518Abstract: Methods are disclosed for rapid, reliable and simple isolation of RNA from formalin-fixed paraffin-embedded tissue samples. RNA purified in this manner can be used for quantitative measurement gene expression levels. The tissue sample can be a tumor or other pathological tissue.Type: GrantFiled: March 1, 2001Date of Patent: September 2, 2003Assignee: University of Sourthern CaliforniaInventors: Kathleen Danenberg, Peter V. Danenberg, Steven Swenson
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Patent number: 6610488Abstract: Methods are disclosed for rapid, reliable and simple isolation of RNA, DNA and proteins from formalin-fixed paraffin-embedded tissue samples. RNA purified in this manner can be used to monitor gene expression levels. The tissue sample can be a tumor or other pathological tissue.Type: GrantFiled: March 1, 2001Date of Patent: August 26, 2003Assignee: University of Southern CaliforniaInventors: Kathleen Danenberg, Peter V. Danenberg, Steven Swenson
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Publication number: 20030100705Abstract: The present invention relates to the use of alkanes for the contamination-free purification or separation of biopolymers.Type: ApplicationFiled: October 22, 2002Publication date: May 29, 2003Inventors: Thomas Rothmann, Roland Fabis, Andreas Schafer, Sabine Dorit Menzel, Thi My Chi Nguyen
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Patent number: 6562952Abstract: A process for forming small micron-sized (1-10 &mgr;m) protein particles is provided wherein a protein, a solvent system for the protein and an antisolvent for the protein solvent system are contacted under conditions to at least partially dissolve the protein solvent system in the antisolvent, thereby causing precipitation of the protein. The solvent system is made up of at least in part of a halogenated organic alcohol, most preferably 1,1,1,3,3,3-hexafluoro-2-propanol (HFIP). Preferably, a solution of the protein in the solvent system is sprayed through a nozzle into a precipitation zone containing the antisolvent (preferably CO2) under near- or supercritical conditions.Type: GrantFiled: October 31, 2000Date of Patent: May 13, 2003Assignee: The University of KansasInventors: Roger A. Rajewski, Bala Subramaniam, William K. Snavely, Fenghui Niu
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Publication number: 20030065152Abstract: The present invention relates to the use of alkanes for the contamination-free purification or separation of biopolymers.Type: ApplicationFiled: May 10, 2002Publication date: April 3, 2003Inventors: Thomas Rothmann, Roland Fabis, Andreas Schafer, Sabine Dorit Menzel, Thi My Chi Nguyen
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Patent number: 6526675Abstract: A method of dewatering fine particulate materials is disclosed. In this method, an aqueous slurry of fine particles is treated with appropriate hydrophobizing reagents so that the particulate material becomes moderately hydrophobic. A lipid of vegetable or animal origin is then added to the slurry in solutions of light hydrocarbon oils and short-chain alcohols, so that the hydrophobic lipid molecules adsorb on the moderately hydrophobic surface and, thereby, greatly enhance its hydrophobicity. By virtue of the enhanced hydrophobicty, the water molecules adhering to the surface are destabilized and more readily removed during the process of mechanical dewatering. The moisture reduction can be further improved using appropriate electrolytes in conjunction with the lipids, spraying surface tension lowering reagents onto the filter cake, subjecting the cake to a suitable vibratory means, and using combinations thereof.Type: GrantFiled: June 7, 1999Date of Patent: March 4, 2003Inventor: Roe-Hoan Yoon
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Patent number: 6518406Abstract: The present invention relates to methods for purification of antithrombin-III (AT-III) by precipitation of impurities. The said methods comprise (a) adding, to a solution comprising antithrombin-III, a saccharide and citrate, in an amount sufficient for impurities to precipitate while antithrombin-III essentially remains in solution; (b) allowing impurities to precipitate; and (c) removing the precipitated impurities, thereby obtaining a solution comprising purified antithrombin-III. The invention also relates to pharmaceutical compositions, obtainable by the said methods, comprising purified antithrombin-III, as well as to reconstituted pharmaceutical compositions essentially free from visible particles.Type: GrantFiled: June 21, 2000Date of Patent: February 11, 2003Assignee: Octapharma AGInventor: Stefan Winge
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Publication number: 20030013641Abstract: Methods are provided for purifying peptides and proteins by incorporating the peptide or protein into a diketopiperazine or competitive complexing agent to facilitate removal one or more impurities, i.e. undesirable components, from the peptide or protein. In a preferred embodiment, a peptide, such as insulin, containing one or more impurities, e.g., zinc ions, is entrapped in diketopiperazine to form a precipitate of peptide/diketopiperazine/impurity, which is then washed with a solvent for the impurity to be removed, which is a nonsolvent for the diketopiperazine and a nonsolvent for the peptide. Formulations and methods also are provided for the improved transport of active agents across biological membranes, resulting for example in a rapid increase in blood agent concentration.Type: ApplicationFiled: August 20, 2002Publication date: January 16, 2003Applicant: Pharmaceutical Discovery Corporation DelawareInventors: Solomon S. Steiner, Rodney J. Woods, Joseph W. Sulner
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Patent number: 6476196Abstract: The present invention is directed to crystals of ER&bgr; ligand binding domain complexed with (1) N-(n-butyl)-11-[3,17&bgr;-dihydroxyestra-1,3,5(10)-trien-7&agr;-yl]N-methylundecanamide; estradiol and a peptide comprising the amino acid sequence LXXLL; or 17-epiestriol and a peptide comprising the amino acid sequence LXXLL.Type: GrantFiled: April 27, 2001Date of Patent: November 5, 2002Assignee: Kara Bio ABInventors: Jan Ljunggren, Ann-Gerd Thorsell, Owe Engstrom, Tomas Bonn, Mats Carlquist, Andrzeji Brzozowski, Ashley Pike, Roderick Hubbard
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Patent number: 6461604Abstract: Crystallographic and NMR solution structures of human IL-6 are reported. The invention provides models and systems incorporating such structures which are useful for identifying IL-6/IL-6 receptor interactions and for identification of agonists and antagonists of such interactions. Crystalline human IL-6 is also provided.Type: GrantFiled: February 7, 2000Date of Patent: October 8, 2002Assignee: Genetics Institute, LLCInventors: William S. Somers, Mark L. Stahl, Jasbir S. Seehra, Guang-Yi Xu, Thomas E. McDonagh, Hsiang-Ai Yu, Jin Hong
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Patent number: 6444211Abstract: Pertactin (formerly 69 kDa protein) is recovered in stable biologically pure form having no detectable adenylate cyclase activity from fermentation broth from the fermentation of Bordetella pertussis as well as from the cells. The broth is processed to selectively remove pertussis toxin (PT) and filamentous haemagglutinin (FHA), the pertactin is precipitated by ammonium sulphate and the precipitate is dissolved in buffer at pH 6.0 to 8.5, the solution then is passed through hydroxyapatite and ion-exchange chromatograph columns before final ultrafiltration. Cells are extracted with urea and the extract ultrafiltered and diafiltered. The pertactin is precipitated from the extract and the precipitate processed as above. In a variation, the broth is contacted with ammonium sulphate to precipitate pertactin, PT and FHA, the precipitate is dissolved and the PT and FHA selectively removed, before the solution is passed to the chromatograph columns.Type: GrantFiled: June 8, 1999Date of Patent: September 3, 2002Assignee: Connaught Laboratories, Inc.Inventors: Gail Jackson, Raafat Fahim, Larry Tan, Pele Chong, John Vose, Michel Klein
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Patent number: 6437101Abstract: Methods are provided in this invention for the isolation of human growth hormone, growth hormone antagonist, or a homologue of either, from a biological source. The methods of the invention use multi-phase extraction.Type: GrantFiled: May 7, 1999Date of Patent: August 20, 2002Assignee: Akzo Nobel N.V.Inventors: Kirk James Hayenga, Pascal P. Valex
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Patent number: 6433144Abstract: This invention relates to methods for isolating highly purified mixtures of natural Type I interferon from white blood cells. The invention also relates to highly-purified mixtures of Type I interferon which resemble natural Type I interferon in that the highly purified mixtures of natural Type I interferon includes at least 9 subtypes, i.e., alpha-1, alpha-2, alpha-5, alpha-7, alpha-8, alpha-10, alpha-14, alpha-21 and omega, giving rise to at least 16, and possibly 20 or more molecular species, including alpha-1a, alpha-1new, alpha-2a, alpha-2b, alpha-2c, alpha-5, alpha-5LG, alpha-7, alpha-8a, alpha-8c, alpha-10a, alpha-14a, alphal4-b, alpha 14-c, alpha-14LG, alpha-21a, alpha-21b, alpha-21c, omega and omega LG.Type: GrantFiled: January 12, 1999Date of Patent: August 13, 2002Assignee: Viragen, Inc.Inventors: Joseph P. Morris, Duy Nguyen, James Kappelman, Michael D. Potter, Mead M. McCabe, Reza Ziai, Stephen Feldman, Hipolito Hartman
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Publication number: 20020099174Abstract: The present invention relates generally to a method of separating one or more components from a protein mixture. More particularly, this invention is directed to a method of separating one or more components of blood plasma comprising one or more filtration steps using a cellulose-based filter aid. The present invention is useful in the preparation of therapeutics, in particular plasma-based therapeutics for use in humans.Type: ApplicationFiled: February 2, 1999Publication date: July 25, 2002Inventors: ANNA JOHNSTON, JEFFERY RAYMOND DAVIES, PETER JAMES TURNER, BRENTON JOHN WILKIE
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Patent number: 6335430Abstract: The invention relates to a process of producing MAP-products from mussel feet. The process is characterised by extracting the mussel feet in a weakly acid aqueous solution containing, for instance, 1-10 percent by weight of a weak acid and 0.5-3 percent by weight of perchloric acid, whereafter the proteins in the aqueous solution are precipitated by adding inorganic or organic salts and separated from the system, subsequent to having extracted the solid substances.Type: GrantFiled: November 28, 2000Date of Patent: January 1, 2002Inventor: Magnus Qvist
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Publication number: 20010034066Abstract: A method of protein precipitation, concentration and removal of non-protein agents from the protein solution wherein the protein solution is treated with a protein-precipitation agent containing an acidic agent, a salt and a precipitate forming agent. After precipitation, the protein precipitate is washed with a water miscible organic solvent agent to remove non-protein agents present in the protein precipitate.Type: ApplicationFiled: April 27, 2001Publication date: October 25, 2001Inventor: Aftab Alam
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Patent number: 6248535Abstract: Methods are disclosed for rapid, reliable and simple isolation of RNA from formalin-fixed paraffin-embedded tissue samples. RNA purified in this manner can be used to monitor gene expression levels. The tissue sample can be a tumor or other pathological tissue.Type: GrantFiled: December 20, 1999Date of Patent: June 19, 2001Assignee: University of Southern CaliforniaInventors: Kathleen Danenberg, Peter V. Danenberg, Steven Swenson
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Patent number: 6239261Abstract: A process for the preparation of a concentrate of von Willebrand factor is described, entailing a solution of a complex of this factor with factor VIII:C being optionally pasteurized and treated with an anion exchanger, there being no binding of the von Willebrand factor.Type: GrantFiled: June 2, 1994Date of Patent: May 29, 2001Assignee: Aventis Behring GmbHInventors: Norbert Heimburger, Gerhard Kumpe, Klaus Wellner
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Patent number: 6177550Abstract: The process of the invention for the extraction of a Growth Factor Complex is characterized in that water is added to natural and growth factors containing material, the pH value is adjusted to 2.5 to 3.2 by the addition of acid, the resulting precipitate is separated from the supernatant, the Growth Factor Complex in the aqueous solution is precipitated by the addition of an organic solvent miscible with water, separated from the liquid phase and dried, and the powder obtained is, if desired, dialyzed.Type: GrantFiled: September 15, 1998Date of Patent: January 23, 2001Assignee: IPR Institute for Pharmaceutical Research AGInventors: Hans Meyer, Hermann Wasmer, Dieter Hofmann
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Patent number: 6166187Abstract: A sample is prepared from blood in a manner which makes it possible to further analyze proteins in the sample, e.g. to detect prions in the sample. Blood is extracted, allowed to clot and subjected to separation processing (e.g. centrifugation) to obtain serum. The serum is treated with a complexing agent which agent binds prions in the sample forming an agent/protein complex which makes it possible to concentrate the complex. Concentration of the complex results in a sample which can be successfully analyzed, e.g. assayed using a range of different types of assay methodologies for detecting prions.Type: GrantFiled: March 5, 1999Date of Patent: December 26, 2000Assignee: The Regents of the University of CaliforniaInventors: Stanley B. Prusiner, Jiri G. Safar
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Protein isolate having an increased level of isoflavone compounds and process for producing the same
Patent number: 6140469Abstract: The present invention relates to the production of an isoflavone enriched vegetable protein isolate in which the weight ratio of material to extractant is controlled and washing of the acid precipitated protein curd is avoided or minimized to provide an increased level of isoflavones in the protein isolate.Type: GrantFiled: October 12, 1993Date of Patent: October 31, 2000Assignee: Protein Technologies International, Inc.Inventors: Jerome L Shen, Balagtas Francisco Guevara, Frank Enrico Spadafora -
Patent number: 6124432Abstract: The present invention aims at providing a method for preparing dermonecrotic toxin, an improved toxoid of dermonecrotic toxin produced by Bordetelia and a toxoid mixture comprising said improved toxoid of dermonecrotic toxin produced by Bordetella and a toxoid of dermonecrotic toxin produced by Pasteurella. There is provided a method for partially purifying dermonecrotic toxin which comprises bringing a dermonecrotic toxin-containing solution into contact with a chromatographic gel sulfated by direct sulfation or a chromatographic gel to which a sulfated molecule is covalently bonded to thereby make the dermonecrotic toxin adsorbed on the gel, and eluting the adsorbed dermonecrotic toxin from the gel.Type: GrantFiled: December 2, 1996Date of Patent: September 26, 2000Assignee: Juridical Foundation The Chemo-Sero-Therapeutic Research InstituteInventors: Toru Kawai, Toshihiro Ushijima, Kozo Takase, Hideo Fujikawa
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Patent number: 6107468Abstract: Disclosed is a method of obtaining a highly soluble protein which method generally includes at least the step of contacting the protein with an amount of antioxidant suitable to raise the solubility of the protein, which method may also be utilized to raise the protein yield of the process. Antioxidants suitable for use in the present invention include substituted and unsubstituted quinones, anisoles, toluenes and tocopherols. Also disclosed is a highly soluble protein which includes a protein and added antioxidant. Further disclosed are food products made from a highly soluble protein. Finally, a method of processing food products is disclosed which at least includes the step of incorporating a highly soluble protein into the food product.Type: GrantFiled: July 6, 1998Date of Patent: August 22, 2000Assignee: Board of Trustees of the University of ArkansasInventor: William L. Boatright
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Patent number: 6080844Abstract: The present invention involves a process of purifying and recovering a recombinant protein from a suspension of cells. The process of the present invention involves extracting a recombinant protein from a concentrated suspension of cells using a water-miscible organic solvent, isolating the recombinant protein from the suspension of cells, concentrating the recombinant protein to remove the water-miscible organic solvent, precipitating the recombinant protein using an acid, washing the recombinant protein with the salt or free form of a suitable organic acid and recovering the recombinant protein.Type: GrantFiled: April 23, 1998Date of Patent: June 27, 2000Assignee: Abbott LaboratoriesInventors: Ronald E. Carney, Joseph Arndt, Julie R. List, Ellen Marie Schwartz
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Patent number: 6051694Abstract: Liquefied gases, compressed gases, and supercritical fluids are used to form protein particles without first dissolving the protein. The product material is expected to retain full activity and be devoid of residual processing chemicals such as solvents, salts, or surfactants.Type: GrantFiled: September 17, 1998Date of Patent: April 18, 2000Inventors: Trevor Percival Castor, Glenn Thomas Hong
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Patent number: 6025146Abstract: The present invention is directed to methods for crystallizing macrophage colony stimulating factor. The present invention is also directed to methods for designing and producing M-CSF agonists and antagonists using information derived from the crystallographic structure of M-CSF. The invention is also directed to methods for screening M-CSF agonists and antagonists. In addition, the present invention is directed to an isolated, purified, soluble and functional M-CSF receptor.Type: GrantFiled: June 5, 1995Date of Patent: February 15, 2000Assignee: Chiron CorporationInventors: Jayvardhan Pandit, Jarmila Jancarik, Sung-Hou Kim, Kirston Koths, Robert Halenbeck, Anna Lisa Fear, Eric Taylor, Ralph Yamamoto, Andrew Bohm
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Patent number: 6019999Abstract: Described is a process for making a liposomal, ion-exchange whey protein and products thereof, which result in the sustained release of amino acids into the body's circulation to generally promote skeletal muscle protein synthesis, decrease body fat in association with diet modification and improve exercise performance. The whey protein is preferably encapsulated in a liposome using a cold, or non-heated, process. After the liposomal, ion-exchange whey protein has been prepared, it is then preferably lyophilized to deliver macronutrients for use as a sports nutrition supplement and for use in medical or clinical catabolic applications.Type: GrantFiled: December 2, 1998Date of Patent: February 1, 2000Inventors: David F. Miller, Ian Hicks, Charles B. Quick, Joey Antonio, Ian J. Reynolds, David Rush, S. Keith Klein, IV
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Patent number: 6005075Abstract: The invention provides processes for producing Alpha-Interferon (IFN-.alpha.) free from possible mouse and/or virus contamination. The present invention further provides homogeneous IFN-.alpha. free from mouse and/or virus contamination and its use in antitumor and/or antiviral treatment.Type: GrantFiled: July 23, 1997Date of Patent: December 21, 1999Assignee: Hoffmann-La Roche Inc.Inventors: Urs Ettlin, Erich Hochuli, Alfred Schacher, Karl Weyer
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Patent number: 5990289Abstract: The instant invention relate to a new method for the purification of proteins using copper chelate-affinity chromatography, wherein the impure or pre-purified protein is adsorbed on immobilized copper(II) ions, optionally washed with buffer and deionized water, washed with a solution of a Lewis-base, and finally eluted with deionized water.Type: GrantFiled: January 2, 1998Date of Patent: November 23, 1999Assignee: Novartis AGInventors: Pierre Fran.cedilla.ois Fauquex, Catherine Georges
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Patent number: 5986073Abstract: A method for purifying and recovering biologically active somatotropin monomers from refold solution following the solubilization and naturation of refractile bodies of host cells produced by recombinant DNA methodology. The purification process is based on the discovery that somatotropin monomers and somatotropin oligomers having overlapping isoelectric points may nevertheless be separated by selective precipitation over a narrow pH range. Host cell residues including proteins, pyrogens and other impurities present in the refold solution are effectively removed in the process. The purified somatotropin monomers recovered from solution after removing precipitated solids are suitable for parenteral application to target animals without further purification.Type: GrantFiled: December 21, 1995Date of Patent: November 16, 1999Assignee: Monsanto CompanyInventors: Stephen B. Storrs, Jeffrey S. Schorey
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Patent number: 5981715Abstract: The present invention is directed to a process for purifying alpha-1-PI. The process comprises providing an impure protein fraction which comprises alpha-1-PI. The impure protein fraction is suspended in an aqueous solution at pH 6. Insoluble proteins are recovered and resuspended in aqueous solution at pH 8.5. PEG is added to precipitate .alpha.-2 proteins. To the PEG supernatant precipitation, which comprises alpha-1-PI, is added ZnCl.sub.2 to precipitate crude alpha-1-PI. The crude alpha-1-PI is resolubilized and applied to an anion-exchange medium. A fraction comprising alpha-1-PI is recovered from the anion-exchange medium. Alpha-1-PI purified by the process has a specific activity about 1.0 units/OD.sub.280.Type: GrantFiled: March 31, 1997Date of Patent: November 9, 1999Assignee: Alpha Therapeutic CorporationInventors: Duk Sung Hwang, Evelyn Nario, Mark Lepe, Lyndon Luz, Hirokazu Ito, Kazuo Takechi
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Patent number: 5981474Abstract: Provided is a method for preparing a true, homogeneous solution of a pharmaceutical substance dissolved in an organic solvent in which the pharmaceutical substance is not normally soluble. Solubilization is obtained by forming a hydrophobic ion pair complex involving the pharmaceutical substance and an amphiphilic material. The resulting organic solution may be further processed to prepare pharmaceutical powders. A biodegradable polymer may be co-dissolved with the pharmaceutical substance and the amphiphilic material and may be incorporated into a pharmaceutical powder. A preferred method for preparing pharmaceutical powders is to subject the organic solution to gas antisolvent precipitation using a supercritical gas antisolvent such as carbon dioxide. Also provided is a method for making hollow particles having a fiber-like shape which would provide enhanced retention time in the stomach if ingested by a human or animal host.Type: GrantFiled: June 17, 1998Date of Patent: November 9, 1999Assignee: University Technology CorporationInventors: Mark C. Manning, Theodore W. Randolph, Eli Shefter, Richard F. Falk, III
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Patent number: 5977324Abstract: A method of concentrating a disease-related conformation of a protein such as the PrP.sup.Sc in a sample is disclosed. The method comprises liquefying the sample and adding a complexing agent such as phosphotungstic acid (PTA) which complexes preferentially or exclusively with the PrP.sup.Sc. After the complex is formed the composition is centrifuged until the complex settles at the bottom. Thereafter, the supernatant is poured away. The remaining pellet may be resuspended in an aqueous solution containing a protease inhibitor for storage. The PTA stains the PrP.sup.Sc making the resulting concentrated PrP.sup.Sc susceptible to further analysis, making it possible to quickly and efficiently determine the presence of PrP.sup.Sc and its concentration in a sample. The method can be used to render a sample non-infectious by removing all or substantial of the infectious form of a protein from a sample.Type: GrantFiled: February 20, 1998Date of Patent: November 2, 1999Assignee: The Regents of the University of CaliforniaInventors: Stanley B. Prusiner, Jiri G. Safar
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Patent number: 5959082Abstract: A new class of proteins and methods related thereto are presented. The proteins, which can be characterized as catalysts of the extension of plant cell walls and the weakening of the hydrogen bonds in pure cellulose, are referred to as expansins. Two proteins have been isolated by fractionation techniques from washed wall fragments of cucumber hypocotyls, referred to as "cucumber expansin-29" and "cucumber expansin-30" (abbreviated cEx-29 and cEx-30, with respect to their apparent relative masses as determined by SDS-PAGE). Moreover, three peptide fragments from the purified cEx-29 protein were sequenced, then oligonucleotide primers were designed to amplify a portion of the expansin cDNA using polymerase chain reaction with a cDNA template derived from cucumber seedlings, and then the PCR fragment was used to screen a cDNA library to identify full length clones.Type: GrantFiled: May 12, 1995Date of Patent: September 28, 1999Assignee: The Penn State Research FoundationInventors: Daniel J. Cosgrove, Simon McQueen-Mason, Mark Guiltinan, Tatyana Shcherban, Jun Shi
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Patent number: 5952470Abstract: A method for separating unmodified hemoglobin from cross-linked hemoglobin in a hemoglobin solution. The method involves contacting the hemoglobin solution with a least one dissociating agent to form a dissociation solution wherein unmodified tetrameric hemoglobin is dissociated to form hemoglobin dimers. The hemoglobin dimers are then separated from the dissociation solution, while retaining the cross-linked hemoglobin in the dissociation solution.Type: GrantFiled: June 7, 1995Date of Patent: September 14, 1999Assignee: Biopure CorporationInventors: William R. Light, Maria S. Gawryl, Anthony J. Laccetti, Robert A. Houtchens