Inorganic Patents (Class 530/420)
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Patent number: 5252216Abstract: This invention relates to the application of combination chromatography to the purification of complement receptor proteins.Type: GrantFiled: March 24, 1992Date of Patent: October 12, 1993Assignee: SmithKline Beecham CorporationInventors: Gail Folena-Wasserman, John H. O'Grady, Thomas M. Smith, John Lifter
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Patent number: 5235041Abstract: Recombinant structural and functional polymers are purified by lysing of the cellular host, separation of the solid materials, washing and extraction of contaminants using a detergent solution at elevated temperatures.Type: GrantFiled: April 13, 1992Date of Patent: August 10, 1993Assignee: Protein Polymer Technologies, Inc.Inventors: Joseph Cappello, Franco A. Ferrari, Tina L. Buerkle, Garret Textor
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Patent number: 5219995Abstract: The present invention describes a process for activating Factor II to Factor II.sub.a by incubating Factor II in the presence of Factor V, Factor X.sub.a, phospholipids, and calcium ions. Each of the factors is prepared from a single impure protein fraction which includes Factors II, V and X. The Factor II, V and X purification procedure comprises the steps of DEAE ligand chromatography and precipitation by the addition of barium chloride. Factor V is recovered from the barium chloride supernatant, and Factors II and X are contained in the barium chloride precipitate. The barium chloride precipitate is dissolved in an aqueous solution and is applied to a chromatographic resin coupled with a ligand which binds Factor X and Factor II weakly or not at all. Factor II is recovered from the fraction, which remains unbound or weakly bound to the Factor X binding ligand. Factor X.sub.Type: GrantFiled: July 14, 1992Date of Patent: June 15, 1993Assignee: Alpha Therapeutic CorporationInventors: Steven W. Herring, Yahiro Uemura, Munehiro Noda, Kenneth T. Shitanishi
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Patent number: 5215963Abstract: A procedure for the preparation of the solubilized and purified gastrin releasing peptide receptor, in an active form, from a gastrin releasing peptide receptor source such as Swiss 3T3 fibroblasts.Type: GrantFiled: October 24, 1989Date of Patent: June 1, 1993Assignee: Berlex Laboratories, Inc.Inventors: Richard I. Feldman, James M. Wu, Elaina Mann, Anne Larocca, James C. Jenson
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Patent number: 5210186Abstract: A method is provided for recovering astaxanthin, astaxanthin carotenoids, astaxanthin esters, chitin and proteins from crustacean tissues containing such. The method comprises an initial extraction of crustacean tissue with boiling lye to form an alkaline extract and an extracted residue. The alkaline extract, upon cooling, forms separate layers from which can be recovered component protein, astaxanthin, astaxanthin carotenoids and astaxanthin esters. The lye extracted residue of chitin-containing such crustacean tissue is readily processed to provide chitin.Type: GrantFiled: July 15, 1991Date of Patent: May 11, 1993Inventors: Gunnar Mikalsen, deceased, by Ester Mikalsen, heiress
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Patent number: 5204447Abstract: Methods for purifying factor XIII from a biological fluid are provided. The methods comprise precipitation of factor XIII by adjusting the pH of the biological fluid to 5.5 to 6.5 and recovering the precipitated factor XIII.Type: GrantFiled: November 14, 1988Date of Patent: April 20, 1993Assignee: ZymoGenetics, Inc.Inventors: Paul D. Bishop, Gerald W. Lasser
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Patent number: 5204452Abstract: A process for inducing flocculation involving the mixing of an aqueous solution of a chitosan salt with a material to be flocculated (e.g., oil, algae, or the like) and then adding a halogenating agent (e.g., sodium hypochlorite) thus forming a N-halochitosan.Type: GrantFiled: November 14, 1990Date of Patent: April 20, 1993Assignee: E. I. Du Pont de Nemours and CompanyInventors: Edward C. Dingilian, George E. Heinsohn
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Patent number: 5182369Abstract: 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: February 28, 1990Date of Patent: January 26, 1993Assignee: Monsanto CompanyInventors: Stephen B. Storrs, Jeffrey S. Schorey
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Patent number: 5177194Abstract: A multi-step process for purifying an immune serum globulin fraction from a crude plasma protein fraction involves precipitating non-serum globulin proteins from an aqueous suspension of the crude plasma protein fraction using a protein precipitant, adding a virus-inactivating agent to the clarified immune serum globulin-containing liquid, absorbing the immune serum globulins onto a cation exchange resin and washing non-serum globulin contaminants from the resin, subjecting the eluate to ultrafiltration to concentrate the immune serum globulins and separate them from low molecular weight species, contacting the concentrate with an anion exchange resin to absorb non-serum globulin contaminants, passing the imune-serum globulins through the anion exchange resin under conditions that leave non-serum globulin contaminants bound to the resin, and subjecting the filtrate to a molecular washing step to produce a purified immune serum globulin fraction.Type: GrantFiled: February 1, 1990Date of Patent: January 5, 1993Assignee: Baxter International, Inc.Inventors: Maria E. Sarno, Clifford Graf, Gerald Neslund, Sau-Gee Yung, James Burnham, Jean Kim, Rodolfo A. Vasquez
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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: 5162506Abstract: The invention relaates to the production of collagen fibers by comminuting collagen containing tissues, drying the comminuted product and milling the dried material while maintaining the temperature sufficiently low to prevent substantial conversion of collagen to gelatin. The collagen fiber product is particularly useful for restructuring poorly textured meats, mechanically recovered meat products, offal, fish, fish products and other protein products to improve textural properties, water retention, fat retention, eating quality, juicines, succulence, shape, size retention and protein content.Type: GrantFiled: July 25, 1990Date of Patent: November 10, 1992Assignee: Natural Resources (Manufacturing) LimitedInventor: Ralph Hadden
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Patent number: 5157113Abstract: An essentially pure and stablized antibody preparation comprising IgM antibodies having a purity greater than about 98% by weight and a nucleic acid content of less than about 200 pg per mg IgM. In one embodiment IgM antibodies from a monoclonal source are subjected to ion exchange and size exclusion chromatography at an alkaline pH to yield a purified IgM having a nucleic acid content of less than 10 pg/mg IgM, preferably less than about 4 pg/mg IgM. A highly purified and stabilized preparation of anti Pseudomonas aeruginosa antibodies is disclosed. The removal of nucleic acids is assured by subjecting the antibody source to at least one and preferably two low pH precipitation steps. In a very preferred embodiment, ion exchange and/or size exclusion chromatography is used to remove any residual nucleic acids.Type: GrantFiled: April 12, 1991Date of Patent: October 20, 1992Assignee: Miles Inc.Inventors: George Dove, Gautam Mitra
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Patent number: 5151500Abstract: A substantially heme-free blood protein product is produced by adding an acid to a blood cell suspension to a low pH to disrupt erythrocytes present in the suspension thereby releasing hemoglobin, and to cleave off the heme moiety from the major proportion of the hemoglobin. The released heme forms a precipitate which is removed by centrifugation. Heme moieties remaining in the blood protein solution are degraded by treatment with an oxidizing agent, e.g. hydrogen peroxide. The product has a content of sulfur-containing amino acids which corresponds to the content thereof in natural hemoglobin, as well as foaming and emulsifying properties corresponding to naural hemoglobin. The product has a high lysine content and may be used to enrich the protein content of edible products, e.g. cereals, or to replace part of the meat in meat products. An edible product containing up to about 25% by weight of blood plasma mixed with the product is also disclosed.Type: GrantFiled: March 29, 1990Date of Patent: September 29, 1992Inventors: Jorgen Wismer-Pedersen, deceased, Jorn Frohlich, legal representative
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Patent number: 5151501Abstract: The present invention relates to a process for solubilization and naturation of somatotropins utilizing a combination of sulfolane and an aqueous alkaline solution. By utilizing the process of the present invention, enhanced yields of end product result.Type: GrantFiled: December 20, 1991Date of Patent: September 29, 1992Assignee: American Cyanamid CompanyInventor: Kevin M. McCoy
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Patent number: 5139937Abstract: A process for producing the protein part of Ca.sup.+2 -binding photoprotein aequorin (apoaequorin) according to a recombinant DNA technique, and a process for purifying the resulting apoaequorin are provided, which production process comprises cultivating a strain having an expression vector piP-HE outside the bacterial bodies transformed into Escherichia coli, followed by separating the resulting culture solution into the bacterial bodies and a culture filtrate, and recovering the culture filtrate, and which purification process comprises adding an acid to the culture filtrate so as to give a pH of 4.7 or less, followed by recovering the resulting white precipitates, dissolving the white precipitates in a buffer solution, reducing the solution, subjecting the resulting apoaequorin fraction to adsorption treatment according to anion exchange chromatography and subjecting the resulting apoaequorin to gel filtration.Type: GrantFiled: November 18, 1988Date of Patent: August 18, 1992Assignee: Chisso CorporationInventors: Satoshi Inouye, Shigeyuki Aoyama, Yoshiyuki Sakaki
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Patent number: 5138030Abstract: A process for extracting type I collagen from an avian source such as poultry feet that incorporates a fibrillar mass of connective tissue as well as bony tissue to yield a collagen product having useful medical and biotechnology applications. In this process, after being cleaned and decontaminated, the poultry feet are comminuted and then enzyme-treated to enhance the yield. The enzyme-treated comminuted material which is rich in collagen is dispersed in an organic acid to cause the fibrillar mass to undergo controlled swelling, after which the mass is separated from the bony tissue and purified to remove non-collangenous material. The purified mass is dried to provide the desired Type I collagen product which may be ground into a powder or formed into a collagen matrix or sponge, depending on the end use therefor.Type: GrantFiled: October 10, 1989Date of Patent: August 11, 1992Inventor: James M. Pachence
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Patent number: 5109119Abstract: This invention provides a crystalline form of recombinant human granulocyte-macrophage colony-stimulating factor (r-h-GM-CSF) and methods for making such crystals.Type: GrantFiled: June 6, 1989Date of Patent: April 28, 1992Assignee: Schering CorporationInventors: Paul Reichert, Gerald S. Hammond, Hung V. Le, Tattanahalli L. Nagabhushan, Paul P. Trotta
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Patent number: 5108908Abstract: A process for pigments such as the treatment of proteinic solutions containing heminic groups or chlorophylls in view of their decolorization, and products thus obtained.The proteinic solution is subjected in a first step, to a slight enzymatic hydrolysis, preferably with acid pH pepsin, and the partially hydrolyzed solution is then brought to a temperature above 60.degree. C., at an acid pH between 2 and 4.Type: GrantFiled: September 14, 1990Date of Patent: April 28, 1992Assignees: Imedex, DibevialInventors: Jacques Coves, Jean-Louis Tayot
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Patent number: 5109121Abstract: 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.Type: GrantFiled: October 9, 1990Date of Patent: April 28, 1992Assignee: Pitman-Moore, Inc.Inventors: Galina Blum, Ren-der Yang, Eun K. Lee
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Patent number: 5101019Abstract: The present invention provides a clear and efficient pertussis endotoxin-removing method characterized in that a fluid containing the antiinfective fraction and endotoxin of strains of phase I Bordetella pertussis is supplied with calcium ion in the presence of excess phosphate ion prior to zonal centrifugation and also a pertussis toxoid whose endotoxin content per 10 .mu.g of proteinic nitrogen is not more than 0.5 ng and its production method.Type: GrantFiled: May 16, 1988Date of Patent: March 31, 1992Assignee: Takeda Chemical Industries, Ltd.Inventors: Isao Fujita, Hideo Watanabe, Masatoshi Miyamoto
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Patent number: 5087695Abstract: An immunoglobulin-rich fraction containing IgG, IgA and IgM is prepared in high concentration (200 mg/ml) by contacting diluted serum with CuSO.sub.4, which is a source of strong positive ions, to produce a precipitate rich in immunoglobulins, whereafter the precipitate is washed with an EDTA chelating agent solution and then a solution of L-lysine.HCl and NaHCO.sub.3 is added to form a colloidal solution of the washed immunoglobulin precipitate.Type: GrantFiled: July 12, 1989Date of Patent: February 11, 1992Assignee: MCY Laboratories Canada, Inc.Inventor: William A. J. McAuley
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Patent number: 5066788Abstract: This invention discloses proteins which inhibit the coagulation of the blood, processes for preparing these proteins, and the use thereof.Type: GrantFiled: December 7, 1989Date of Patent: November 19, 1991Assignee: Boehringer Ingelheim International GmbHInventor: Christian M. Reutelingsperger
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Patent number: 5066787Abstract: This invention discloses proteins which inhibit the coagulation of the blood, processes for preparing these proteins, and the use thereof.Type: GrantFiled: November 23, 1987Date of Patent: November 19, 1991Assignee: Boehringer Ingelheim International GmbHInventor: Christian P. M. Reutelingsperger
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Patent number: 5059680Abstract: A preparation of an isolated immunoreactive CA 125 Antigen, and a method of isolating it is disclosed. CA 125 Antigen is a glycoprotein having a molecular weight of about 200kD, and a carbohydrate-content of about 24%. The CA 125 Antigen is isolated from a cell culture medium by acid precipitation, and is subsequently purified by size exclusion chromatography and immunoaffinity chromatography.Type: GrantFiled: November 24, 1986Date of Patent: October 22, 1991Assignee: Centocor, Inc.Inventors: Hugh M. Davis, Thomas L. Klug, Vincent R. Zurawski, Jr.
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Patent number: 5055555Abstract: A process for purifying human G-CSF from an aqueous solution including the step of adding NaCl to the solution to selectively precipitate the human G-CSF.Type: GrantFiled: January 5, 1989Date of Patent: October 8, 1991Inventor: Helmut Sassenfeld
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Patent number: 5047504Abstract: A process for isolating and purifying GM-CSF produced from recombinant sources. The process provides for the isolation and purifying of recombinant GM-CSF produced in E. coli.Type: GrantFiled: February 17, 1989Date of Patent: September 10, 1991Assignee: Amgen, Inc.Inventor: Thomas C. Boone
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Patent number: 5045453Abstract: The present invention provides a method for extracting lipid bound sialic acid from a sample of blood plasma or serum and determining the amount of sialic acid present in the sample which comprises:(a) adding to the sample a mixture of a lower alkyl alcohol and a chlorinated lower alkyl hydrocarbon so as to form a resulting admixture, the volume ratio of the lower alkyl alcohol to the chlorinated lower alkyl hydrocarbon being in the range from about 70:30 to about 85:15;(b) mixing the resulting admixture for a period of time sufficient to dissolve lipid bound sialic acid present in the sample;(c) treating the admixture so as to form a recoverable, substantially clear lipid bound sialic acid-containing upper phase;(d) separately recovering from the clear upper phase so formed a predetermined volume of the upper phase; and(e) determining the amount of lipid bound sialic acid present in the predetermined volume of the upper phase and thereby the amount of sialic acid present in the sample.Type: GrantFiled: August 26, 1988Date of Patent: September 3, 1991Assignee: Dianon Systems, Inc.Inventor: Nonda Katopodis
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Patent number: 5011914Abstract: A ciliary neurotrophic factor (CNTF), particularly sciatic nerve CNTF (SN-CNFT) is claimed. The SN-CNTF described herein is a single protein species and has a specific activity that increased to greater than 25,000-fold from crude extract. The purification is carried out by lowering the pH of the crude nerve extract preparation to form a precipitate which is removed and discarded; raising the pH to about 6.3 followed by ammonium sulfate fractionation; chromatofocusing a solution containing a second precipitate obtained from the 30% to 60% ammonium sulfate containing solution; subjecting the fractions obtained by chromatofocusing to sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE); and performing reversed-phase high-performance liquid chromatography (HPLC) on the SDS-PAGE eluate.Amino acid data for this SN-CNTF is also provided. In addition, methods for using this data for providing SN-CNTF probes and for screening cDNA and genomic libraries are also provided.Type: GrantFiled: January 5, 1989Date of Patent: April 30, 1991Inventors: Franklin D. Collins, Leu-Fen Lin
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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: 4988798Abstract: 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.Type: GrantFiled: January 22, 1990Date of Patent: January 29, 1991Assignee: Pitman-Moore, Inc.Inventors: Galina Blum, Ren-der Yang, Eun K. Lee
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Patent number: 4966963Abstract: A method for the preparation of proteins in biologically active form including providing a source of protein solubilized from inclusion bodies with a cationic surfactant; providing a weak denaturing agent; and contacting the solubilized protein with the weak denaturant in water in an amount sufficient to allow the protein to remain in a biologically active form.Type: GrantFiled: February 11, 1988Date of Patent: October 30, 1990Assignee: Bunge (Australia) Pty. Ltd.Inventor: Joseph J. Patroni
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Patent number: 4958007Abstract: A method is provided for extracting human interleukin-4 (IL-4) from IL-4 expressing bacterial cells. The method comprises treating the bacterial cells with a deactivating agent, disrupting the cell membrane and recovering the IL-4.Type: GrantFiled: May 17, 1988Date of Patent: September 18, 1990Assignee: Schering-Plough Corp.Inventors: Yair Alroy, Paul Leibowitz
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Patent number: 4956278Abstract: Anaplasma marginale antigen, antigen compositions, vaccine and process for the production of said antigen, antigen composition and vaccine are disclosed. The Anaplasma marginale is free of the erythrocyte antigens that cause neonatal isoerythrolysis, and effective as a vaccinate which will not only protect the vaccinate against bovine anaplasmosis, but does not induce neonatal isoerythrolysis in offspring of vaccinates.Type: GrantFiled: February 23, 1988Date of Patent: September 11, 1990Assignee: Louisiana State UniversityInventors: Lewis T. Hart, Donald G. Luther, William J. Todd
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Patent number: 4937324Abstract: Proteins having therapeutic potential as both anticoagulants and as anti-inflammatory agents are disclosed. The present invention also discloses the use of lipocortins in reducing blood coagulation in warm-blooded animals.Type: GrantFiled: February 4, 1988Date of Patent: June 26, 1990Assignees: ZymoGenetics, Inc., The Board of Regents of the University of WashingtonInventors: Kazuo Fujikawa, Meher H. Irani, Bruce L. A. Carter
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Patent number: 4923967Abstract: 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.Type: GrantFiled: September 26, 1988Date of Patent: May 8, 1990Assignee: Eli Lilly and CompanyInventors: Jesse L. Bobbitt, Joseph Manetta
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Patent number: 4902782Abstract: Basic Fibroblast Growth Factor (FGF) is substantially purified by the employment of affinity chromatography using heparin-linked support material. Described is a simplified three step procedure for extracting basic FGF from either mammalian brain or mammalian pituitary tissue. Salt precipitation, e.g., with ammonium sulfate is used to provide a partially purified precipitate that is then subjected to ion-exchange chromatography, e.g., using a Carboxymethyl-Sephadex column. Substantially pure basic FGF fractions are then obtained by fractionating the further partially purified fractions using affinity chromatography on a heparin-linked support e.g., Heparin-Sepharose.Type: GrantFiled: November 7, 1988Date of Patent: February 20, 1990Assignee: The Salk Institute for Biological StudiesInventors: Denis Gospodarowicz, Andrew Baird, Peter Bohlen
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Patent number: 4894440Abstract: A megakarytocyte stimulatory factor (MSF), purified to homogeneity, is an acidic protein (pI=5.1) with an Mr=15,000 which stimulates PF4-like protein synthesis in rat promegakaryoblast cells by as much as 7-fold, and exhibits half-maximal activity at a concentration of 0.8 pM. MSF exhibits no biologic activity corresponding to other known hemopoietic growth factors, and appears to be specific for the megakaryocyte lineage.In the given examples, MSF was purified to homogeneity (as judged by SDS-PAGE and isoelectric focusing in the presence of 9.2 M urea) from serum-free conditioned medium obtained from cultured human embryonic kidney (HEK) cells, and to near homogeneity from thrombocytopenic plasma.Type: GrantFiled: September 17, 1986Date of Patent: January 16, 1990Assignee: Massachusetts Institute of TechnologyInventor: Robert D. Rosenberg
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Patent number: 4885236Abstract: A biochemical procedure for identification and characterization of cells in a biopsy or sample of a body fluid. The method can be used to determine cell type, i.e. epidermal, neuronal; tissue of origin, i.e. breast tissue, liver tissue; and degree of abnormality. The procedure can also be used to make antibodies and hybridization probes to detect cell or tissue specific antigens and nuclear matrix associated nucleic acids in cellular material and body fluids.The procedure is based on the isolation and analysis of the components of a specific subcellular protein fraction referred to here as the "nuclear matrix". The nuclear matrix includes proteins and nuclear matrix associated DNA specific to different cell types. These proteins and nucleic acids are altered or new ones expressed as a result of viral infection, genetic defects or malignancy.Type: GrantFiled: December 23, 1986Date of Patent: December 5, 1989Assignee: Massachusetts Institute of TechnologyInventors: Sheldon Penman, Edward G. Fey
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Patent number: 4883865Abstract: A liquid phase containing preS2+S antigen is separated into two phases after which the desired antigen is concentrated, washed and adsorbed and desorbed from a fumed silica to produce a product that is purified and concentrated in antigen:protein ratio and that is suitable for final purification.Type: GrantFiled: September 30, 1987Date of Patent: November 28, 1989Assignee: Merck & Co. Inc.Inventor: Dennis J. Kubek
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Patent number: 4882268Abstract: A biochemical procedure for diagnosis of three important properties of cells in a biopsy or blood sample: tumor type i.e., the tissue type that has become neoplastic; tissue of origin if the tumor has arisen from a metastasis; and degree of malignancy. The procedure can also be used to obtain antibodies which can be used to determine tissue of origin by immunostaining and to detect tumor antigens appearing in blood by radioimmunoassay.The procedure consists of isolating and analyzing components of a specific subcellular fraction referred to here as the "nuclear matrix". The nuclear matrix consists of proteins specific to different cell types and nuclear matrix associated DNA. The electrophoretic pattern of the proteins and restriction endonuclease digested DNA is unique and reproducible within a particular cell type and is therefore useful in diagnosing cell type. Changes in these patterns following transformation to a malignant phenotype provide additional diagnostic information.Type: GrantFiled: December 24, 1985Date of Patent: November 21, 1989Assignee: Massachusetts Institute of TechnologyInventors: Sheldon Penman, Edward G. Fey
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Patent number: 4861383Abstract: This invention provides a process for easily recovering nearly white starch and protein having a high commercial value by depressing darkening of crushed slurry and juice in producing starch and protein of a subterranean stem.The above-mentioned process is characterized by adding at least one member selected from the group consisting of sodium thiosulfate, potassium thiosulfate, sodium hydrogen sulfite, sodium sulfite and potassium sulfite at the time of crushing the subterranean stem.Type: GrantFiled: September 29, 1987Date of Patent: August 29, 1989Assignee: Hitachi, Ltd.Inventors: Masahiko Ishida, Ryooichi Haga, Yoji Odawara, Sankichi Takahashi, Katsuya Ebara
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Patent number: 4816400Abstract: Basement membrane collagen degrading enzymes are provided which are useful for the detection of malignant cells with metastatic activity. Means for detecting such cells are also provided.Type: GrantFiled: June 26, 1987Date of Patent: March 28, 1989Inventors: Karl Tryggvason, Lance A. Liotta
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Patent number: 4795698Abstract: A magnetic-polymer particle, useful in immunoassay techniques and various other biological/medical applications is produced by coprecipitation of transition metals in the presence of a polymer having available coordination sites. These particles are capable of forming stable aqueous suspensions and may be easily resuspended after agglomeration.Type: GrantFiled: September 16, 1986Date of Patent: January 3, 1989Assignee: Immunicon CorporationInventors: Charles S. Owen, John C. Silvia, Louis D'Angelo, Paul A. Liberti
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Patent number: 4785079Abstract: Basic Fibroblast Growth Factor (FGF) is substantially purified by the employment of affinity chromatography using heparin-linked support material. Described is a simplified three step procedure for extracting basic FGF from either mammalian brain or mammalian pituitary tissue. Salt precipitation, e.g., with ammonium sulfate is used to provide a partially purified precipitate that is then subjected to ion-exchange chromatography, e.g., using a Carboxymethyl-Sephadex column. Substantially pure basic FGF fractions are then obtained by fractionating the further partially purified fractions using affinity chromatography on a heparin-linked support e.g., Heparin-Sepharose.Type: GrantFiled: December 10, 1986Date of Patent: November 15, 1988Assignee: The Salk Institute for Biological StudiesInventors: Denis Gospodarowicz, Andrew Baird, Peter Bohlen
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Patent number: 4774019Abstract: An apparatus is provided for reacting a solution of a precipitating medium of alkaline metal chlorides at a fixed rate of delivery with plasma continuously separated from blood, filtering the precipitate formed by the reaction, removing the solution of precipitating medium from the plasma following the use of the medium, adjusting the purified treated plasma, and returning the purified plasma to the blood in an amount equivalent to that of the continuously separated plasma. To enhance the precipitative separating action of alkaline metal chloride on plasma protein without detracting from the advantages of the alkaline metal chloride, use is made of a solution of precipitating medium comprising a mixture of the alkaline metal chloride and an amino acid, the latter being added in an amount sufficient to promote the precipitating effect of the alkaline metal chloride.Type: GrantFiled: March 17, 1987Date of Patent: September 27, 1988Assignee: Terumo Kabushiki KaishaInventors: Masaharu Watanabe, Hiroaki Ohe
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Patent number: 4771125Abstract: Human soluble immune response suppressor (SIRS) having a molecular weight of about 10,000 to 15,000, an isoelectric point of about 7 and a defined amino acid composition distinctly different from murine SIRS is produced from a culture of MOLT-4 cells.Type: GrantFiled: April 10, 1986Date of Patent: September 13, 1988Inventors: H. William Schnaper, Thomas M. Aune
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Patent number: 4743583Abstract: Lewis acid-Lewis base high molecular weight salt microparticulate material of the type referred to in U.S. Pat. No. 3,959,457, which include biologically active peptides and proteins solubilized in a non-aqueous, non-denaturing manufacturing solvent.Type: GrantFiled: July 20, 1987Date of Patent: May 10, 1988Assignee: Temple UniversityInventors: Tully J. Speaker, Tycho J. Speaker
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Patent number: 4736018Abstract: This invention discloses proteins which inhibit the coagulation of the blood, processes for preparing these proteins, and the use thereof.Type: GrantFiled: September 23, 1985Date of Patent: April 5, 1988Assignee: Boehringer Ingelheim International GmbHInventor: Christian P. M. Reutelingsperger
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Patent number: 4732891Abstract: Novel human placenta-derived anticoagulating substances having the following properties:(1) molecular weight of 34,000.+-.2,000 determined by SDA-polyacrylamide gel electrphoresis under reduced state;(2) isoelectric point of 4.7.+-.0.1 determined by isoelectric column electrophoresis using an ampholite;(3) stabilityinactivated by heat treatment at 50.degree. C. to 30 minutes, stable at a pH of 4-10, and stable in plasma at 37.degree. C. for 30 minutes;(4) activitycapable of prolonging a recalcification time, a prothrombin time, and an activated partial thromboplastin time; and(5) the existence of several amino acids including aspartic acid, threonine, serine, and so on; are prepared by homogenizing human placenta, subjecting the resulting homogenate to centrifugal separation, extracting an anticoagulating substance from the residue or from a microsome fraction contained in the supernatant with a surface active agent and/or a chelating agent, and purifying and isolating the substance from the extract.Type: GrantFiled: September 19, 1986Date of Patent: March 22, 1988Assignee: Kowa Co., Ltd.Inventors: Masahiro Maki, Hideo Tani
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Patent number: 4731440Abstract: A method for solubilization and naturation of somatotropin protein from refractile bodies of host cells is disclosed. The method embraces the discovery that an aqueous solution of urea, or dimethylsulfone, or mixtures of urea and dimethylsulfone, can be effectively used to solubilize refractile bodies containing such somatotropin protein. Once solubilized, somatotropin protein can be natured in an aqueous solution of urea, or dimethylsulfone, or mixtures of urea and dimethylsulfone, by contacting the solution with a mild oxidizing agent for a time sufficient to result in the formation of the disulfide bonds. Naturation can efficiently occur even at high protein concentration, in an impure preparation and in the absence of reducing agent.Type: GrantFiled: August 25, 1986Date of Patent: March 15, 1988Assignee: Monsanto CompanyInventors: Larry A. Bentle, James W. Mitchell, Stephen B. Storrs, Grant T. Shimamoto