Chromatography Or By Septum Selective As To Material, E.g., Gel Filtration, Molecular Sieve Dialysis, Etc. Patents (Class 530/417)
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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: 5312628Abstract: A method of isolating soluble pancreatic islet antigen employs extraction with a non-ionic detergent and fractionation on a gel filtration column. Fractions are screened for high immunoreactivity with diabetic serum which is positive for ICA immunofluorescence when tested on tissue sections of a pancreas from a human blood group O donor. The isolated soluble antigen is suitable for measuring autoantibodies in both complement fixation assays as well as ELISA-type and immunoblotting formats. Methods of using isolated soluble antigen to test serum for autoantibodies are also taught.Type: GrantFiled: May 12, 1993Date of Patent: May 17, 1994Assignee: Exocell, Inc.Inventors: Margo P. Cohen, Van-Yu Wu
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Patent number: 5310878Abstract: A biosynthetic cerebrospinal fluid control and method of use. Additionally, this invention relates to the isolation and purification of stable liquid human prealbumin, a component in the biosynthetic cerebrospinal fluid control.Type: GrantFiled: October 23, 1992Date of Patent: May 10, 1994Assignee: Baxter Diagnostics Inc.Inventor: Kathryn D. Herring
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Patent number: 5306426Abstract: The invention features a method of detecting a trace solute in a solution which contains a major amount of a dissolved product, the method including the steps of: flowing the solution through means for extracting the product to produce an effluent flow substantially free of product containing the trace solute; flowing the effluent through a trace solute adsorbing means to progressively accumulate therein the trace solute; and eluding the trace solute from the adsorber to produce an eluant fraction containing a detectable quantity of the trace solute.Type: GrantFiled: May 25, 1993Date of Patent: April 26, 1994Assignee: Perseptive Biosystems, Inc.Inventor: Noubar B. Afeyan
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Patent number: 5304638Abstract: A separation medium for use in protein separation comprising a water-insoluble matrix carrying a plurality of polyamine groupings, the polyamine groupings having at least three basic nitrogen atoms, the basic nitrogen atoms being separated from each other by a chain of at least two intervening carbon atoms, there being a total of 5 such intervening carbon atoms when there is a total of three nitrogen atoms in each polyamine group, which may be used for at least partially purifying factor VIII.Type: GrantFiled: December 4, 1991Date of Patent: April 19, 1994Assignee: Central Blood Laboratories AuthorityInventors: Philip J. Marshall, Christopher R. Lowe
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Patent number: 5304603Abstract: The present invention relates to a compound which when administered to Leydig cells in the testes stimulates the production of androgen such as testosterone. This compound, when mixed with other known compounds, can produce testosterone levels in excess of those obtained by the administration of a maximal stimulatory dose of Lutenizing Hormone (LH).Type: GrantFiled: June 18, 1991Date of Patent: April 19, 1994Assignee: The Population CouncilInventors: C. Yan Cheng, C. Wayne Bardin
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Patent number: 5304637Abstract: Methods are provided for improved production of hIL-3 either in glycosylated form from mammalian and yeast cells or in unglycosylated form from prokaryotes. Recombinantly produced human IL-3 is purified in a series of steps, initially employing hydrophobic interaction, followed by ion exchange chromatography and gel filtration.Type: GrantFiled: March 13, 1990Date of Patent: April 19, 1994Assignee: Gist-brocades N.V.Inventors: Lambertus C. J. Dorssers, Gerard Wagemaker, Yvonne J. Vos, Robert W. Van Leen, Maria L. N. Persoon
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Patent number: 5302699Abstract: Disclosed is an antitumorigenic protein derived from fruit bodies of matsutake mushrooms (Tricholoma matsutake). Also disclosed is a method of preparing the antitumorigenic protein comprising extracting fruit bodies of matsutake mushrooms with water followed by subjecting the resulting extract to purification composed of combination of the following three purifying steps in any desired order:(1) a step of purifying the protein by molecular sieve chromatography in a gel permeation column;(2) a step of bringing the extract in contact with an anion exchange resin so that the protein is adsorbed to the resin followed by eluting the protein from the column of the resin with an eluent; and(3) a step of bringing the extract in contact with a hydrophobic chromatographic resin so that the protein is adsorbed to the resin followed by eluting the protein from the column of the resin with an eluent.Type: GrantFiled: January 22, 1993Date of Patent: April 12, 1994Assignees: Director of National Food Research Institute, Ministry of Agriculture, Forestry and Fisheries, Momoya Co., Ltd.Inventors: Yukio Kawamura, Akihiro Morita, Makoto Tomatsu, Masaru Ishikawa
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Patent number: 5296592Abstract: Mammalian Interleukin-1 receptor proteins (IL-1Rs), DNAs and expression vectors encoding mammalian IL-1Rs, and processes for producing mammalian IL-1Rs as products of cell culture, including recombinant systems, are disclosed.Type: GrantFiled: March 1, 1993Date of Patent: March 22, 1994Assignee: Immunex CorporationInventors: Steven K. Dower, Carl J. March, John E. Sims, David L. Urdal
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Patent number: 5294700Abstract: The disclosure describes novel immunosuppressive agents isolated from syncytiotrophoblast microvilli membranes by preparing a minutely subdivided and solubilized preparation of said membranes and isolating the unreduced N-linked oligosaccharides from an extract of said preparation.Type: GrantFiled: January 4, 1993Date of Patent: March 15, 1994Assignee: Monsanto CompanyInventors: Peter D. Arkwright, Raymond A. Dwek, Christopher W. G. Redman, Graham A. W. Rook, thomas W. Rademacher
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Patent number: 5294336Abstract: Stable hemoglobin A.sub.lc (s-A.sub.lc) can be separated from other hemoglobin components and quantitated in a short time by means of a liquid-chromatographic apparatus comprising a separation column packed with a packing material consisting essentially of a porous substance having a carboxyalkyl group combined thereinto, as ion exchanger, a means for injecting a sample into the separation column, a means for passing one or more eluents through the separation column, and a means for detecting hemoglobin, hemoglobin derivatives or glycosylated hemoglobin, the average particle size of the packing material in dry state being 4 .mu.m or less.Type: GrantFiled: June 9, 1992Date of Patent: March 15, 1994Assignee: Hitachi, Ltd.Inventors: Masako Mizuno, Kenji Tochigi, Yutaka Misawa, Hiroyuki Miyagi, Yoshio Watanabe, Taro Nogami, Junkichi Miura, Yoshinori Takata
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Patent number: 5292663Abstract: An eliminating agent used for the measurement of the amount of glycosylated hemoglobins in a blood sample is provided. The eliminating agent comprises condensed phosphoric acids and/or the salts thereof as the main ingredient, wherein the agent eliminates labile glycosylated hemoglobin A.sub.1c into non-glycosylated hemoglobin and glucose. There is also provided a reagent comprising the eliminating agent and a hemolysis agent, which is used for the measurement of the amount of glycosylated hemoglobins; and an eluent comprising the eliminating agent, which is used for the separation of glycosylated hemoglobins in blood samples by ion-exchange chromatography to measure the amount of the glycosylated hemoglobins. A method for measuring the amount of glycosylated hemoglobin A.sub.1c in a blood sample involves the use of the eliminating agent, the reagent comprising the eliminating agent and the hemolysis agent, and/or the eluent.Type: GrantFiled: May 3, 1993Date of Patent: March 8, 1994Assignee: Sekisui Kagaku Kogyo Kabushiki KaishaInventors: Kazutoshi Yamazaki, Masahiro Takechi, Toshiki Kawabe, Masayuki Yokoi
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Patent number: 5290920Abstract: Human epidermal growth factor is provided in an ultrapure form characterized by the absence of protein contaminants detectable by capillary electrophoresis analysis. A method for obtaining such ultrapure human epidermal growth factor includes fractionation of a human epidermal growth factor preparation by reversed phase high performance liquid chromatography in the presence of a cationic ion-pairing agent.Type: GrantFiled: April 16, 1992Date of Patent: March 1, 1994Assignee: Allelix Biopharmaceuticals Inc.Inventors: Dennis R. Sindrey, Chandra M. Dwivedi
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Patent number: 5288708Abstract: A new substance BPC; the process for its preparation from human and animal gastric juice comprising purifications steps: centrifugalization, dialysis, ion-exchange, chromotagraphy, gal chromatography and lyophilisation; a drug for human and veterinary use and a process for the treatment of stress-induced diseases and disorders, inflammation and edemas, diseases and disorders of dopaminergic etiology, for treatment of diabetes mellitus, diseases and disorders of gastrointestinal tract, heart, kidney, pancreas, liver, testis, hematopoetic, skeletal and nervous, system, dementias, wound, burns, fracture, viral diseases, malignancy; in surgery; some disorders of fertility and immune system; protection against ionizing radiation; for veterinary use in commercial breeding.Type: GrantFiled: May 10, 1991Date of Patent: February 22, 1994Inventors: Predrag Sikiric, Marijan Petek, Ivo Rotkvic, Stjepan Mise, Simun Krizanac, Ivan Udovicic, Ernest Suchanek, Marko Duvnjak, Jerka Jukic
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Patent number: 5288856Abstract: A method of isolating cystine rich acid-stable, biologically active proteins comprising the steps of co-precipitation by acidification of said proteins together with at least one acid-sensitive protein; isolation of said proteins from the co-precipitate by its resuspension in aqueous solution and the subsequent recovery of the proteins from the supernatant.Type: GrantFiled: March 19, 1992Date of Patent: February 22, 1994Inventor: Pierre Amiguet
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Patent number: 5286849Abstract: The present invention relates to a process for purifying Factor IX from an impure protein fraction containing Factor IX. The purification process comprises the steps of adding a solvent and a detergent to an impure protein fraction and incubating the solvent/detergent protein solution to inactivate any viral contaminants. Factor IX is purified from the solvent/detergent protein solution by chromatography on a sulfated polysaccharide resin without first removing the solvent and detergent prior to the purification on the sulfated polysaccharide resin. The Factor IX, purified by the process has a specific activity of at least 85 units/mg.Type: GrantFiled: July 14, 1992Date of Patent: February 15, 1994Assignee: Alpha Therapeutic CorporationInventor: Steven W. Herring
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Patent number: 5284934Abstract: The present invention provides a process for preparing a carbohydrate-binding lectin derivative for use as immune modulators or immunoconjugates. The polymer-lectin conjugate produced in accordance with the process is polyethylene glycol Ricinus communis agglutinin I (PEG-RCAI). The lectin is coupled to the polymer by activating the polymer with a coupling agent such as 1,1-carbonyldiimidazole. The polymer-lectin conjugate is biologically active, biocompatible and is expected to be substantially non-immunogenic.Type: GrantFiled: September 4, 1992Date of Patent: February 8, 1994Assignee: Health Research Inc.Inventor: Howard J. Allen, Jr.
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Patent number: 5276142Abstract: A process for extracting and purifying a protein having an apparent molecular weight of about 69,000 daltons from the outer membrane of the bacterium Bordetella pertussis is provided. The process includes inactivating Bordetella pertussis cells with a bacteriostatic agent, repetitive extraction, and purification of the 69,000 dalton protein from extract by dye ligand chromatography followed by chromatofocusing. The process results in improved yield and stability of the 69,000 dalton protein.Type: GrantFiled: December 11, 1989Date of Patent: January 4, 1994Assignee: American Cyanamid CompanyInventor: John W. Gotto
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Patent number: 5266205Abstract: A method of separating solute material from a polar fluid in a first polar fluid phase is provided. The method comprises combining a polar fluid, a second fluid that is a gas at standard temperature and pressure and has a critical density, and a surfactant. The solute material is dissolved in the polar fluid to define the first polar fluid phase. The combined polar and second fluids, surfactant, and solute material dissolved in the polar fluid is maintained under near critical or supercritical temperature and pressure conditions such that the density of the second fluid exceeds the critical density thereof. In this way, a reverse micelle system defining a reverse micelle solvent is formed which comprises a continuous phase in the second fluid and a plurality of reverse micelles dispersed in the continuous phase. The solute material is dissolved in the polar fluid and is in chemical equilibrium with the reverse micelles. The first polar fluid phase and the continuous phase are immiscible.Type: GrantFiled: July 1, 1992Date of Patent: November 30, 1993Assignee: Battelle Memorial InstituteInventors: John L. Fulton, Richard D. Smith
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Patent number: 5259951Abstract: A method for the purification of Factor VIII from human plasma is described, wherein a solution comprising Factor VIII is purified by using ion exchange chromatographic columns. Factor VIII obtained by said method is also described.Type: GrantFiled: June 11, 1991Date of Patent: November 9, 1993Assignee: SCLAVO S.p.A.Inventors: Silvana Arrighi, Maria G. Borri, Costante Ceccarini
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Patent number: 5258496Abstract: Methods are provided for the isolation and purification of recombinant lung surfactant protein. The methods involve a multistep procedure including extraction with a C.sub.1 -C.sub.4 aliphatic alcohol and chromatographic purification steps which employ a C.sub.1 -C.sub.4 aliphatic alcohol as eluant. Purified proteins obtained using the disclosed isolation and purification steps are provided as well.Type: GrantFiled: July 10, 1990Date of Patent: November 2, 1993Assignee: Scios Nova Inc.Inventors: Bradley J. Benson, Douglas Buckley, David Lesikar, Asha Naidu, Kate B. Silverness
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Patent number: 5258504Abstract: The invention relates to a process for the purification of streptolysin O (SLO) by means of chromatography and to the use of streptolysin.Type: GrantFiled: October 8, 1992Date of Patent: November 2, 1993Assignee: Behringwerke AktiengesellschaftInventors: Harald Althaus, Peter Merle
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Patent number: 5256769Abstract: A protein of interest or a Met-protein, e.g. the N-Met analog of the protein of the interest can be efficiently separated from a mixture thereof by subjecting the mixture to a separation procedure utilizing the difference in the isoelectric points between the protein and the Met-protein.Type: GrantFiled: September 11, 1985Date of Patent: October 26, 1993Assignee: Takeda Chemical Industries, Ltd.Inventors: Koichi Kato, Takao Yamada, Kenji Kawahara
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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: 5252217Abstract: The invention relates to a human Factor XI concentrate having high specific activity prepared using a process comprising a filtration-adsorption step and a single step of chromatography on cation exchange resin.The concentrate obtained is perfectly suitable for therapeutic use in replacement therapy in cases of Factor XI deficiency.Type: GrantFiled: May 7, 1992Date of Patent: October 12, 1993Assignee: Association pour l'Essor de la Transfusion Sanguine dans la Region du NordInventors: Miryana Burnouf-Radosevich, Dominique Dernis
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Patent number: 5245014Abstract: A method for isolating Factor VIII from other proteins dissolved in blood plasma is disclosed, wherein plasma is subjected to gel filtration under group separation conditions giving a fraction containing Factor VIII in very high yield and almost free of other proteins.Type: GrantFiled: November 7, 1990Date of Patent: September 14, 1993Assignee: Novo Nordisk A/SInventor: Per Kaersgaard
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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: 5240859Abstract: The present invention provides methods and reagents for sequencing amino acids. One embodiment of the method for determining the terminal amino acid of a substantialy pure polypeptide comprises the steps of (a) attaching the polypeptide to a solid support, (b) reacting the polypeptide with a compound described below, under conditions and for a time sufficient for coupling to occur between the terminal amino acid of the polypeptide and the compound, thereby yielding a polypeptide with a derivatized terminal amino acid, (c) washing the solid support to remove unbound material, (d) cleaving the derivatized terminal amino acid from the polypeptide with a cleaving agent, (e) ionizing the cleaved derivatized terminal amino acid, and (f) determining the molecular weight of the derivatized terminal amino acid, such that the terminal amino acid is determined.Within one embodiment, the compound is p-isothiocyanato phenethyl trimethylammonium and counterion salts thereof.Type: GrantFiled: February 22, 1991Date of Patent: August 31, 1993Assignee: B.R. Centre LimitedInventor: Rudolf H. Aebersold
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Patent number: 5238925Abstract: Disclosed herein is purified isolated angiogenic factor, isolated from Live Yeast Cell Derivative. Also disclosed herein are methods to treat mammals suffering from wounds or burns comprising administering the angiogenic factor and pharmaceutical formulations for use in the methods.Type: GrantFiled: May 9, 1990Date of Patent: August 24, 1993Assignee: The State of Oregon Acting by and through The State Board of Higher Education on Behalf of the Oregon Health Sciences UniversityInventor: J. Peter Bentley
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Patent number: 5234991Abstract: A porous mineral support such as a porous mineral oxide coated with an aminated polysaccharide polymer has cationic characteristics and is capable of reversibly fixing thereto biological macromolecules. This material is employed in the separation and purification of said biologic macromolecules.Type: GrantFiled: March 17, 1987Date of Patent: August 10, 1993Assignee: Pasteur Merieux Serums and VaccinesInventors: Jean-Louis Tayot, Michel Tardy
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Patent number: 5235043Abstract: This invention describes processes for producing mature human members of the NGF/BDNF family of neurotrophic proteins that are fully biologically active. In addition, the gene encoding human BDNF and processes for obtaining the same are disclosed.A previously-unreported member of the NGF/BDNF family of neurotrophic proteins, NGF-3, has been identified and a portion of the gene encoding for the NGF-3 has been described. Processes for identifying additional previously unreported members of the NGF/BDNF family are also described.Type: GrantFiled: October 9, 1990Date of Patent: August 10, 1993Assignee: Synergen, Inc.Inventors: Frank Collins, Susan Bektesh, Tadahiko Kohno, Jack Lile
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Patent number: 5229493Abstract: A novel growth factor (BTC-CG) was purified from the conditioned medium of pancreatic beta tumor cells initially derived from transgenic mice (RIPl-Tag2). The purification scheme included BioRex 70 chromatography, phenyl-Sepharose chromatography, TSL-GEL heparin FPLC and C4 reverse phase HPLC. The peptide also stimulated proliferation of bovine smooth muscle cells. It was not inactivated by boiling, by 10 mM dithiothreitol or by exposure to IM acetic acid. Biological activity of BTC-GF was recovered from a single band of protein which had a molecular weight of 2,000 on SDS-PAGE. The Partial N-terminal amino acid sequence of this protein was determined with an ABI 470A protein sequencer as: Asp-Gly-[X]-Thr-[X]-Arg-Thr-Pro-Glu-[X]-Asn-Gly.Type: GrantFiled: October 26, 1990Date of Patent: July 20, 1993Assignee: Children's Medical Center CorporationInventors: Moses J. Folkman, Yuen Shing
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Patent number: 5229498Abstract: A method is provided for cleansing a protein from multivalent metal ions bound thereto, these ions being released from the protein by exchanging the ions with monovalent metal ions, whereafter the multivalent metal ions are removed. The release and removal of these ions is effected, in particular, by diafiltration or gel filtration processes.Type: GrantFiled: December 24, 1991Date of Patent: July 20, 1993Assignee: Kabi Pharmacia ABInventor: Rainer Eketorp
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Patent number: 5223435Abstract: Sequential degradation of peptides for sequencing purposes by successive cleavage of amino acids from one end of the peptide chain is performed in an adsorption column with flows of the degradation reagents and wash liquids passing through the column in both directions. Migration of the peptide in one direction is thereby compensated by a subsequent migration in the other, and loss of peptide from the column over repeated cleavages is avoided. In preferred embodiments, the column contains two serially arranged adsorbent zones with differing adsorption characteristics, and the directions of flow of the various system components through the column are selected with a view toward a difference in peptide partitioning between the stationary and mobile phases in one zone vs. the other. The result is that any migration of the peptide occurring at any stage of a given cycle of the procedure occurs at a greater rate toward the zone interface than away from it.Type: GrantFiled: October 25, 1991Date of Patent: June 29, 1993Assignee: Genetech, Inc.Inventor: William J. Kohr
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Patent number: 5221734Abstract: A Milk Growth Factor (MGF) obtained from milk, methods for its isolation and purification from milk or milk products, pharmaceutical compositions, food compositions and cell growth media comprising the factor and the uses thereof for treating trauma in mammals, suppressing the immune response, treating cancer, stimulating growth of mammals and cell cultures.Type: GrantFiled: March 16, 1992Date of Patent: June 22, 1993Assignee: Ciba-Geigy CorporationInventors: Robert R. Burk, David Cox
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Patent number: 5219993Abstract: The EPI protein is isolated and purified from a fermentation solution, using chromatographic technique, wherein the solution containing the EPI protein is applied to a matrix coupled with heparin, preferably heparin-Sepharose.Type: GrantFiled: August 12, 1991Date of Patent: June 15, 1993Assignee: Novo Nordisk A/SInventors: Ole Nordfang, Soren Carlsen
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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: 5219926Abstract: A process for covalently bonding biopolymer, such as protein, to an organic polymer surface coated with hydrophilic nonionic polymer having groups reactive with the biopolymer and having a cloud point in the reaction medium that is at least 5.degree. C. above the temperature at which the coated organic polymer surface is to be used, which comprises reacting biopolymer with the surface in an aqueous reaction medium, at a temperature not less than 5.degree. C. below the cloud point; but not above a temperature at which the biopolymer is deleteriously affected, and preferably not above about 100.degree. C., the product comprises a biopolymer immobilized on a hydrophilic solid surface having a nonionic polymer and a hydrophilic layer, coupled thereto via biopolymer-reactive groups of the nonionic polymer, and accordingly has low spontaneous adsorption of proteins and other biopolymers through electrostatic attraction and/or hydrophobic interaction.Type: GrantFiled: September 13, 1991Date of Patent: June 15, 1993Assignee: Berol Nobel ABInventors: Bjorn Lindman, Martin Malmsten, Krister Holmberg, Carina Andren
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Patent number: 5219999Abstract: Crude immunoglobulin G isolated from human blood plasma is treated according to a conventional technique (such as the tricalcium phosphate adsorption method) to remove aggregates therefrom to such an extent that they are not detectable by gel filtration analysis. In order to produce an aqueous solution of immunoglobulin G having a reduced anticomplementary activity, the resulting solution is then filtered through a porous polyolefin membrane having a pore size larger than the molecular size of immunoglobulin G, in the presence of a stabilizer having surface activity. The aqueous solution of immunoglobulin G so produced is suitable for use in intravenous injection because its anticomplementary activity is low.Type: GrantFiled: March 15, 1991Date of Patent: June 15, 1993Assignees: Mitsubishi Rayon Co., Ltd., The Japanese Red Cross SocietyInventors: Tohru Suzuki, Hiroyuki Ikeda, Kazuyo Ikeda, Tsugikazu Tomono, Sadayoshi Sekiguchi, Takeji Ohtani, Seigi Suzuki
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Patent number: 5218094Abstract: A novel neuronotrophic factor having a molecular weight of about 14,000 to 17,000 daltons and an isoelectric point of about 10 is prepared by homogenization of mammalian brain tissue, particularly bovine brain tissue, acid precipitation of the homogenate thus produced, dialysis of the resulting supernatant with dialysis membranes having a molecular weight cut-off of between 5 and 10 kilodaltons and chromatographic fractionation upon molecular weight permeation of the dialyzed supernatant thus produced. The neuronotrophically active fractions may be further purified by cation exchange chromatography with a gradient of ammonium acetate buffer. The neuronotrophic factor of the invention is useful in the treatment of various neuropathological conditions.Type: GrantFiled: August 2, 1990Date of Patent: June 8, 1993Assignee: Fidia, S.p.A.Inventor: Francesco della Valle
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Patent number: 5208021Abstract: A potent and specific immunotoxin is prepared by coupling an inactivated diphteria toxin to a binding moiety such as a monoclonal antibody or transferrin. The immunotoxins are specific for human tumors and leukemias and are indistinguishable in cell toxicity from that of the native toxin linked to the binding domain without the toxicity to other cells. The immunotoxin is useful in treating graft versus host disease as well as selectively killing tumor cells, such as medulloblastoma and glioblastoma cells.Type: GrantFiled: January 25, 1989Date of Patent: May 4, 1993Assignees: The United States of America as represented by the Secretary of the Department of Health and Human Services, Cetus CorporationInventors: Virginia G. Johnson, Larry Greenfield, Richard J. Youle, Walter Laird
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Patent number: 5208219Abstract: Activin is administered systemically and locally to induce the growth of mature bone. Activin enhances the level of bone formation and the quality of the bone formed when administered locally with BMP or bone marrow. Administration of activin by subcutaneous route promotes systemic increase in the bone mass.Type: GrantFiled: February 14, 1991Date of Patent: May 4, 1993Assignee: Celtrix Pharmaceuticals Inc.Inventors: Yasushi Ogawa, David K. Schmidt, Rosa Armstrong, Ranga Nathan, Andrea Y. Thompson, Saeid M. Seyedin
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Patent number: 5204257Abstract: A method of recovering nucleic acid-containing particles from a liquid medium by contacting the liquid medium containing the particles with a mixture of hydroxylated silica beads and a salt solution to bind the nucleic acid-containing particles, centrifuging the mixture to pellet the bound particles, and separating the pellet from the liquid.Type: GrantFiled: April 29, 1991Date of Patent: April 20, 1993Assignee: Autogen Instruments, Inc.Inventors: David A. DeBonville, Kelley A. Logan
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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: 5202421Abstract: This invention relates to a novel glycoprotein with anticoagulant activity in human urine, a process for its preparation and a pharmaceutical composition comprising the said glycoprotein for the prevention and/or treatment of diseases related to the disorders in the blood coagulation system.Type: GrantFiled: December 26, 1989Date of Patent: April 13, 1993Assignee: Mochida Pharmaceutical Co., Ltd.Inventors: Yasuyuki Kunihiro, Ryo Tanaka, Michio Ichimura, Akio Uemura, Nobuo Ohzawa, Ei Mochida
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Patent number: 5198538Abstract: The disclosure describes novel immunosuppressive agents isolated from syncytiotrophoblast microvilli membranes by preparing a minutely subdivided and solubilized preparation of said membranes and isolating the unreduced N-linked oligosaccharides from an extract of said preparation.Type: GrantFiled: December 9, 1991Date of Patent: March 30, 1993Assignee: Monsanto CompanyInventors: Peter D. Arkwright, Raymond A. Dwek, Christopher W. G. Redman, Graham A. W. Rook, Thomas W. Rademacher
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Patent number: 5196352Abstract: A new homogeneous cytosolic binding (HCB) protein, having a specific binding activity of about 26 .mu.g FK-506 per mg protein and a molecular weight of about 10-12 kilodaltons, reversibly binds the immunosuppressant FK-506 but not cyclosporine A (CSA). The protein is stable to heating at 56 degrees C. for 30 minutes retaining its FK-506 binding affinity, and has the (partial) amino terminal amino acid sequence: H.sub.2 N G y V l G n V l G u T r I e S r P o G y A p G y A g T r P e P o L s A g-Gly-Gln-Thr-X-Val-Val-Val-His-Tyr-Thr-Gly-Met-Leu-Glu-Asp-Fly-Lys-Phe-AS p (wherein X is undefined). The HCBV protein is isolated from the cytosol of mammalian tissues, preferably human neoplastic T-cell lines, e.g. Jurkat, and can be used in diagnostic and purification procedures involving FK-506 macrolide type immunosuppressants. The HCB protein also catalyses the cis-trans isomerization of proline-containing peptide bonds.Type: GrantFiled: June 27, 1991Date of Patent: March 23, 1993Assignee: Merck & Co., Inc.Inventors: John J. Siekierka, Hsuen-Yun Hung, Marie J. Staruch, Nolan H. Sigal, Richard A. Mumford
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Patent number: 5190658Abstract: An apparatus and a method for size exclusion chromatography is provided. The apparatus is a chromatographic column adapted for use in size exclusion chromatography by having dimensions suitable for size exclusion chromatography and by having a packing material comprising generally spherical particles having wedge-shaped macropores. Preferred particles are in the shape of lamellar and/or acicular crystals extending radially outwardly from a central core region and comprise aluminum oxide, aluminum hydroxide or a mixture thereof. The method involves passing a solution of macromolecules through a column adapted for size exclusion chromatography packed with such particles. The particles effectively and efficiently separate a wide range of macromolecules in decreasing order of their molecular weight.Type: GrantFiled: February 3, 1992Date of Patent: March 2, 1993Assignee: Monsanto CompanyInventors: Lev Z. Vilenchik, Roger C. Ayotte, Jawed Asrar, Christopher J. Hardiman
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Patent number: 5190752Abstract: An intravenously administrable polyclonal immunoglobulin preparation for the treatment and prophylaxis of bacterial infections containing at least 50% by weight of IgM in terms of the total content of immunoglobulin, exhibiting a low anticomplementary activity, being stable in aqueous solution, and being free of viruses. It can also consist of or also contain a mixture of several monoclonal IgM antibodies. The source material for its manufacture is an immunoglobulin-containing fraction of human, animal, or bacterial provenance. The fraction is treated with an anion exchanger that is eluted with a saline or pH gradient and the eluate is optionally subjected to gel filtration, treated before or after the chromatography with .beta.-propiolactone and PEG 4000, and optionally heated. Treatment with .beta.-propiolactone and ultraviolet light, treatment with solvents and detergents, or pasteurization can also be conducted. Proteins, sugars, or mixtures of amino acids are optionally added to the preparation.Type: GrantFiled: July 14, 1989Date of Patent: March 2, 1993Assignee: Biotest Pharma GmbHInventors: Wolfgang Moller, Hebert Dichtelmuller, Norbert Kothe, Dieter Rudnick, Detlef Piechaczek
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Patent number: 5187260Abstract: A process is disclosed in which high purity protamine-DNA complexes are prepared by collecting nucleoprotamines specific developmental stages of a life form, specifically, amphibian, egg by low temperature processing. The process also includes the steps of sequential homogenization in a high concentration aqueous salt solution at a buffered low pH, followed by ultracentrifugation to remove insoluble matter. Either a crude mixture or pure isolate of the complexes may be produced. Pure isolates require aqueous chloroform extraction to isolate protein and to remove lipids. Lyophilization then removes chloroform and excess water. The isolate is then fractionated by single pass alumina chromatography. Dialysis against pure water removes salts. Repeated lyophilization removes excess water and concentrates single protamines and protamine-like proteins. The mixture may then be reconstituted with 5% weight/volume heterologous or homologous DNA, in order to shield from charge toxicity.Type: GrantFiled: April 15, 1991Date of Patent: February 16, 1993Inventors: Sharifa Karali, John K. Barberii