Ultra Filtration Or Osmosis Patents (Class 530/414)
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Patent number: 5527770Abstract: An immunotherapeutic agent is prepared from cells of E. coli or members of the genus Mycobacterium. The material is effective as an anti-tumor agent, an immunostimulant, and an adjuvant. Also disclosed is a method of evoking an immunostimulatory response through the activation of the RAS gene.Type: GrantFiled: August 31, 1994Date of Patent: June 18, 1996Assignee: International Gene Group, Inc.Inventor: David Platt
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Patent number: 5521287Abstract: Human serum albumin obtained by gene manipulation techniques can be purified by a combination of specified steps in which a culture supernatant obtained from a human serum albumin-producing host is subjected to ultrafiltration, heat treatment, acid treatment and another ultrafiltration, followed by subsequent treatments with a cation exchanger, a hydrophobic chromatography carrier and an anion exchanger, and by salting-out to thereby obtain a pure form of human serum albumin which contains substantially no proteinous and polysaccharide contaminants, which is formulated into a pharmaceutical preparation. The thus obtained human serum albumin can further be purified by treating recombinant human serum albumin with a hydrophobic chromatography carrier at pH of 2 to 5 and a salt concentration of 0.4 to 1 and exposing the carrier to a pH of 6 to 8 and a salt concentration of 0.01 to 0.Type: GrantFiled: February 25, 1994Date of Patent: May 28, 1996Assignee: The Green Cross CorporationInventors: Takao Ohmura, Akinori Sumi, Wataru Ohtani, Naoto Furuhata, Kazuya Takeshima, Kaeko Kamide, Munehiro Noda, Masahide Kondo, Syoichi Ishikawa, Kazuhiro Oohara, Kazumasa Yokoyama, Nagatoshi Fujiwara
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Patent number: 5484887Abstract: Interleukin 1 has been purified by use of various techniques including ion exchange chromatography and dye-ligand affinity chromatography. By these techniques, interleukin 1 has been purified to homogeneity. The high purification of interleukin 1 has enabled the amino acid composition of this protein to be ascertained and its amino acid sequence to be partially determined.Type: GrantFiled: November 30, 1984Date of Patent: January 16, 1996Assignee: Immunex CorporationInventors: Shirley R. Kronheim, Carl J. March, Paul J. Conlon, III, Thomas P. Hopp
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Patent number: 5476922Abstract: Autocrine growth factors and isoforms of those factors have been identified, isolated, purified and manipulated. Nucleic acid segments coding for the factors, and antibodies directed to the factors are also aspects of the present invention. The effect of these growth factors on cells is to enhance their growth by increasing mitogenesis. In particular, the growth factors stimulate kidney epithelial cell growth. The growth factors differ from others previously reported in their molecular weights and other properties, for example, resistance to denaturation by dithiothreitol. Methods of preparation and use of the factors are also described. The growth factors are released from kidney epithelial cells by short exposures to a low-sodium environment. The factors have potential for treatment of kidney disease.Type: GrantFiled: September 22, 1993Date of Patent: December 19, 1995Assignee: ARCH Development CorporationInventors: F. Gary Toback, Margaret Walsh-Reitz, Stephen L. Gluck
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Patent number: 5470954Abstract: A process for purifying Factor VIII:C comprising contacting an immobilized antibody specifically binding a Factor VIII:C with Factor VIII: C, desorbing Factor VIII:C from the antibody which had adsorbed it, eluting Factor VIII:C from the presence of the antibody, passing the eluted Factor VIII:C through an affinity region capable of binding the Factor VIII:C, binding the Factor VIII:C in the affinity region and passing contaminants through said region, and eluting the purified Factor VIII:C.Type: GrantFiled: October 21, 1993Date of Patent: November 28, 1995Assignee: Baxter International Inc.Inventors: Gerard G. Neslund, Shu-Len Liu, Michael J. Griffith
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Patent number: 5468844Abstract: An improvement is provided in a process for the membrane filtration of a protein solution. The improvement consists of applying a high shear force at the surface of the membrane. In embodiments of such process, the liquid is subjected to membrane filtration utilizing a rotating membrane disc mounted in close proximity e.g., about 1/8" to about 1/4" to a stationary solid disc, or a rotating solid disc mounted in close proximity e.g., about 1/8" to about 1/4" to a stationary membrane surface with the relative rotation being between bout 1,000 and about 3,450 RPM. This results in permeation characteristics of the selected membrane which essentially represents its theoretical molecular weight cut-off.Type: GrantFiled: January 7, 1994Date of Patent: November 21, 1995Assignee: Protose Technologies Inc.Inventor: Paul Smith
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Patent number: 5466781Abstract: A process is described for producing M-CSF from bacteria. It includes: fermentation of bacteria containing M-CSF DNA; harvest of the fractions that contain the M-CSF protein (refractile bodies); primary recovery of the protein; solubilization and denaturation of refractile bodies; M-CSF refolding; purification by column chromatography and other methods; and formulation of the properly refolded M-CSF. This method is advantageous over prior methods in terms of yield and purity.Type: GrantFiled: March 8, 1993Date of Patent: November 14, 1995Assignee: Chiron TherapeuticsInventors: Glenn Dorin, David R. Gray, Byeong S. Chang, Cynthia A. Cowgill, Robert J. Milley
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Patent number: 5464939Abstract: A substantially pure non-glycosylated human interleukin-2 protein having a specific activity of not less than 10.sup.4 U/mg is obtained by growing a transformant carrying a DNA having a base sequence coding for human interleukin-2 to cause production and accumulation of human interleukin-2 in the culture broth, subjecting the thus obtained human interleukin-2-containing liquid to a purification process comprising a hydrophobic column chromatography.Type: GrantFiled: September 9, 1992Date of Patent: November 7, 1995Assignee: Takeda Chemical Industries, Ltd.Inventors: Kato Koichi, Yamada Takao, Onda Haruo
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Patent number: 5461034Abstract: A biochemically pure polypeptide(s), termed osteogenic growth polypeptide (OGP), which exhibits stimulatory effects on osteoblastic cells, in vivo bone formation and hemopoietic reconstruction. OGP, identified from regenerating bone marrow, has an amino acid sequence ofAla-Leu-Lys-Arg-Gln-Gly-Arg-Thr-Leu-Tyr-Gly-Phe-Gly-Gly.Type: GrantFiled: June 18, 1993Date of Patent: October 24, 1995Assignee: Yissum Research Development Company of the Hebrew University of JerusalemInventors: Gideon A. Rodan, John W. Jacobs, Mohinder K. Sardana, Dan Gazit, Michael Chorev, Andras Muhlrad, Arye Shteyer, Nura Mansur, Zvi Greenberg, Shimon Slavin, Olga Gurevitch, Itai A. Bab
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Patent number: 5459052Abstract: Ala-Glu-IGF-I is a novel compound which exerts IGF-I activity and is a precursor for the preparation of IGF-I. Ala-Glu-IGF-I may by converted to IGF-I by renaturation after recombinant production in E. coli under specified conditions and then cleaving Ala-Glu from the IGF-I.Type: GrantFiled: July 2, 1993Date of Patent: October 17, 1995Assignee: Novo Nordisk A/SInventors: Lars Skriver, Kim R. Hejn s, Henrik Dalboge
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Patent number: 5455331Abstract: Whey protein fractions, especially alpha-lactalbumin and beta-lactoglobulin, are produced by a process which comprises the steps of: (a) treating the whey to achieve a reduction in the specific gravity and ionic strength of the whey to levels which should not be less than 25% of their original values; (b) adjusting the pH of the whey to a value in the range 3.80 to 5.50 by the addition of acid; the above steps being carried out in any order; (c) heating the pH-adjusted whey to a temperature in the range 55.degree.-70.degree. C., and maintaining the whey at that temperature for a period greater than 30 seconds and sufficient to permit aggregation of a portion of the protein content of the whey; (d) cooling the whey to a temperature less than 55.degree. C.Type: GrantFiled: June 15, 1993Date of Patent: October 3, 1995Assignee: Commonwealth Scientific and Industrial Research OrganisationInventor: Robert J. Pearce
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Patent number: 5453363Abstract: A process for the activation of t-PA or IgG after expression in prokaryotes is described. The process includes cell digestion, solubilization under denaturing and reducing conditions and activation under oxidizing conditions in the presence of GSH/GSSG.Type: GrantFiled: March 2, 1994Date of Patent: September 26, 1995Assignee: Boehringer Mannheim GmbHInventors: Rainer Rudolph, Stephan Fischer, Ralf Mattes
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Patent number: 5453490Abstract: A method for the production of commercial quantities of highly purified interleukin-1 inhibitor (IL-1i) from a recombinant host is disclosed. A preferred recombinant E. coli host for use in this method is also disclosed.Type: GrantFiled: August 30, 1994Date of Patent: September 26, 1995Assignee: Synergen, Inc.Inventors: Robert Hageman, Stephen P. Eisenberg, David Dripps, Ronald Evans, Henryk Cudny, Robert C. Thompson
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Patent number: 5447853Abstract: A method of producing a useful high-molecular-weight substance by culturing animal cells capable of proliferation, which comprises (A) a culturing step of culturing said animal cells in suspension to form a suspension culture mixture containing the animal cells and a useful high-molecular-weight substance produced by the animal cells; (B) a separating step of separating the animal cells from the suspension culture mixture and withdrawing the culture medium; (C) a removing step of removing low-molecular-weight substances inhibiting the growth of the animal cells from the culture medium, said inhibitor substances being the metabolites of the animal cells and different from the useful high-molecular-weight substance; (D) a recycling step of recycling part or the whole of the culture medium left after removal of the growth-inhibiting low-molecular-weight substances to the culturing step (A); and (E) a recovering step of recovering the useful high-molecular-weight substance accumulated in the culture system.Type: GrantFiled: April 17, 1992Date of Patent: September 5, 1995Assignee: Teijin LimitedInventors: Michiyuki Tokashiki, Kimihiko Hamamoto
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Patent number: 5444159Abstract: 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: November 6, 1992Date of Patent: August 22, 1995Assignee: Connaught Laboratories LimitedInventors: Gail Jackson, Raafat Fahim, Larry Tan, Pele Chong, John Vose, Michel Klein
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Patent number: 5440018Abstract: Human serum albumin obtained by gene manipulation techniques can be purified by a combination of specified steps in which a culture supernatant obtained from a human serum albumin-producing host is subjected to ultrafiltration, heat treatment, acid treatment and another ultrafiltration, followed by subsequent treatments with a cation exchanger, a hydrophobic chromatography carrier and an anion exchanger, and by salting-out to thereby obtain a pure form of human serum albumin which contains substantially no proteinous and polysaccharide contaminants, which is formulated into a pharmaceutical preparation. This process makes it possible to effeciently purify recombinant human serum albumin and to provide substantially pure human serum albumin which does not contain producer host-related substances and other contaminants and is sufficiently free from coloration.Type: GrantFiled: March 24, 1993Date of Patent: August 8, 1995Assignee: The Green Cross CorporationInventors: Takao Ohmura, Akinori Sumi, Wataru Ohtani, Naoto Fuluhata, Kazuya Takeshima, Kaeko Kamide, Munehiro Noda, Masahide Kondo, Syoichi Ishikawa, Kazuhiro Oohara, Kazumasa Yokoyama
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Patent number: 5430129Abstract: The invention pertains to pure, native dystrophin of mammalian skeletal muscle and a method of purifying dystrophin from mammalian skeletal muscle. The invention further pertains to a method of diagnosing muscular dystrophy by detecting the loss or abnormal structure of pure, native dystrophin from mammalian skeletal muscle. The detection of a loss of dystrophin or an abnormal structure of dystrophin is indicative of muscular dystrophy.Type: GrantFiled: January 16, 1991Date of Patent: July 4, 1995Assignee: University of Iowa Research FoundationInventors: Kevin P. Campbell, Steven D. Kahl, James M. Ervasti
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Patent number: 5410021Abstract: The protein/starch bond is broken mechanically by wet attrition milling rather than by cooking or with chemicals alone. The grain particles are milled to a particle size sufficiently small to break the bond between starch and protein and sufficiently large to retain substantially all of the starch granules intact. The protein is then extracted with ethanol and alkali solvents, separated and dried to form protein and/or protein isolate. The intact starch granules are cleaned and dried.Type: GrantFiled: September 1, 1992Date of Patent: April 25, 1995Assignee: Energenetics, Inc.Inventor: Willem H. Kampen
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Patent number: 5408041Abstract: The present invention relates to the development of bone growth factors as therapeutics for the prevention and treatment of pathological conditions involving bone tissue. The present invention provides biologically active proteinaceous factors comprising polypeptides containing the amino acid sequence M-A-G-L-G-D-E-F-G-D, [SEQ ID NO: 1], (X) F E T L F G A/V E D V I/D A L Q F V C G D, [SEQ ID NO: 2], or A-Y-I-P-I-E-T-L-E-G-I/G-E-L-V-D/Q-T-G/L-Q-F, [SEQ ID NO: 3], or biologically active fragments or sequence analogues thereof. Among the biological properties of the proteinaceous materials of the present invention is the capability to promote the growth and/or differentiation of osteoblastic cells.Type: GrantFiled: January 13, 1994Date of Patent: April 18, 1995Assignees: Rhone-Poulenc Rorer Pharmaceuticals Inc., OsteoSA Inc.Inventors: Gregory R. Mundy, Gloria E. Gutierrez, Ian R. Garrett, Massimo Sabatini, Elzbieta Izbicka, Wilson Burgess, Gregg R. Crumley, Clarence C. Morse, Timothy R. Arnett
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Patent number: 5371191Abstract: A method for purifying bone-derived osteoinductive factors including an ultrafiltration process, an anion exchange process, a cation exchange process, and a reverse phase HPLC process. The ultrafiltration process preferably includes a first ultrafiltration step using a membrane having a nominal molecular weight cutoff of approximately 100 kilodaltons (kD) and a second ultrafiltration step employing a membrane having a nominal molecular weight cutoff of approximately 10 kD. For the anion exchange process, a strongly cationic resin is used, preferably having quaternary amine functional groups. Typically, the eluant for the anion exchange process has a conductivity from about 10,260 micromhos (.mu.mhos) (1.026.times.10.sup.-2 siemens (S)) to about 11,200 .mu.mhos (1.120.times.10.sup.31 2 S). For the cation exchange process, a strongly anionic resin is used, preferably having sulfonic acid functional groups. The eluant for the cation exchange process typically has a conductivity from about 39,100 .mu.mhos (3.91.Type: GrantFiled: October 26, 1993Date of Patent: December 6, 1994Inventors: James W. Poser, James J. Benedict
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Patent number: 5359032Abstract: This invention relates to interleukin inhibitors (IL-1 INHs) that selectively inhibit interleukin 1 activity. The invention also relates to processes for purifying such IL-1 INHs from urine and for producing such IL-1 INHs by hosts transformed with recombinant DNA molecules comprising DNA sequences encoding the inhibitors, and to methods of treatment and compositions characterized by such IL-1 INHs. These methods and agents are useful in immunosuppressive and anti-inflammatory applications and therapies.Type: GrantFiled: December 1, 1992Date of Patent: October 25, 1994Assignee: Biogen Inc.Inventors: Jean M. Dayer, Philippe L. Seckinger, Gonzalo J. Mazzei, Alan R. Shaw
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Patent number: 5340734Abstract: A process for the in vitro production of chemically modified polyphenolic polymer (PPP). First, stable, highly active extracellular tyrosinase is produced from genetically transformed microorganism such as Streptomyces antibioticus. The tyrosinase is then incubated with a reaction substrate such as l-tyrosine, hydrolyzed protein, or an oligopeptide in combination with l-tyrosine. The ratio of the oligopeptide/tyrosine combination as well as variation in the concentration of tyrosinase can be used to modify the color, the molecular size, and the spectral absorbance properties of the PPP produced. Alternatively, or additionally, oxidants such as hydrogen peroxide or hypochlorite can be used to modify the color of the PPP, regardless of the method used to produce the PPP, and the PPP can subsequently be fractionated using molecular weight cut-off ultrafiltration. Organic solvents can also be used in the method of making PPP to produce PPPs having variable but reproducible physical properties.Type: GrantFiled: November 25, 1992Date of Patent: August 23, 1994Assignee: Biosource Genetics CorporationInventors: Guy R. della-Cioppa, Stephen J. Garger, Jr., Richard B. Holtz, Michael J. McCulloch, Genadie G. Sverlow
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Patent number: 5324822Abstract: A method of isolation of a material with similar immunological properties to CA-195 from human amniotic fluid has been disclosed. This material can be substituted for CA-195 in many processes, for example in the preparation of analytical control materials.Type: GrantFiled: December 21, 1992Date of Patent: June 28, 1994Assignee: Ciba Corning Diagnostics Corp.Inventor: Thomas H. Duffy
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Patent number: 5310877Abstract: The invention is directed to a method for the separation of gamma globulin from albumin contained in an aqueous solution of both having a pH of 8-10 by ultrafiltration using an altered substrate microfilter having a water permeability of no more than 20 gallons per square foot per day per pound per square inch.Type: GrantFiled: April 8, 1993Date of Patent: May 10, 1994Assignee: E. I. Du Pont de Nemours and CompanyInventor: Harold G. Spencer
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Patent number: 5292869Abstract: The present invention relates to a method for isolating and purifying transferrin and lactoferrin receptor proteins from bacterial pathogens by affinity chromatography and to the preparation of vaccine antigens containing the purified receptor proteins.Type: GrantFiled: April 11, 1990Date of Patent: March 8, 1994Assignee: The Board of Governors of the UniversityInventor: Anthony B. Schryvers
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Patent number: 5259971Abstract: The present invention relates to a method of purifying native, intact fibrinogen from a liquid sample containing contaminants having molecular weights higher and/or lower than that of the fibrinogen. The method comprises subjecting the sample to filtration using one or more filters having a molecular weight cut-off such that the native, intact fibrinogen is separated from the contaminants.Type: GrantFiled: March 2, 1992Date of Patent: November 9, 1993Assignee: CryoLife, Inc.Inventors: Brenda Smith Morse, Henry B. Kopf
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Patent number: 5248769Abstract: A refractile material containing a heterologous protein is recovered from a host microorganism cell culture transformed to produce the protein. One recovery process involves first reducing the ionic strength of the culture medium prior to disruption to a level effective in preventing reaggregation of cellular debris with refractile material after disruption, disrupting the desalted culture, optionally adding material to the disruptate to create a density or viscosity gradient and separating the refractile material from the cellular debris by high-speed centrifugation. Preferably the salt removal step is carried out by diafiltration and the heterologous protein comprises recombinant M-CSF, IL-2 or IFN-.beta..Type: GrantFiled: November 25, 1991Date of Patent: September 28, 1993Assignee: Cetus Oncology CorporationInventor: Glenn Dorin
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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: 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: 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: 5198213Abstract: Whey derived from ordinary milk includes a bottom fraction including lactose and minerals, a middle fraction including lower molecular weight proteins, and a top fraction including higher molecular weight proteins. The top whey fraction includes a measurable but low level concentration of immunologically active immunoglobulin plus other pathogen specific antibodies. The whey is ultrafiltered through one or more different process steps to yield a filtered product having a concentration of immunologically active immunoglobulin of at least about seven percent of total solids. The filtered product is periodically tested to verify its activity to a specified microbe. The filtered product is orally administered in a therapeutically effective dose to an animal to treat a disease.Type: GrantFiled: October 16, 1991Date of Patent: March 30, 1993Assignee: Protein Technology, Inc.Inventors: Gerald H. Stott, David O. Lucas
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Patent number: 5194591Abstract: A method of producing a whey protein concentrate rich in immunoglobulins which comprises fractionating whey proteins into an immunoglobulin rich fraction and an immunoglobulin depleted fraction and concentrating at least the immunoglobulin rich fraction, in which either (i) a protein containing liquid selected from the group consisting of a whey, a liquid whey protein concentrate or a reconstituted whey protein concentrate powder is subjected to ultrafiltration through a membrane having a molecular weight cut-off of substantially 500,000 whereby to directly produce an immunoglobulin enriched concentrate together with fat, the permeate containing at least a major proportion of the remaining whey proteins, or (ii) a protein containing liquid selected from the group consisting of a whey, a liquid whey protein concentrate or a reconstituted whey protein concentrate powder is subjected to the action of an anion-exchange resin to produce an effluent, the whey proteins in which contain a higher proportion of immunogType: GrantFiled: December 5, 1988Date of Patent: March 16, 1993Assignee: Express Foods Europe LimitedInventor: Robin C. Bottomley
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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
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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: 5173415Abstract: A membrane filter of 0.025 to 0.05 .mu. in pore size is treated by passing the solution of a water-soluble high molecular substance such as albumin, dextran, polyvinylpyrrolidone, polysorbate 80, gelatin or the like through the membrane filter. Employing the filter thus treated, the solution of a physiologically active substance of human origin such as human growth hormone, kallikrein, trypsin inhibitor, epidermal growth factor, leucocyte interferon etc. is filtered at high recovery rate of the active substance avoiding the adsorption of the active substance onto the filter. By the filtration, harmful viruses such as Creutzfeldt-Jacob disease pathogen which may exist in the physiologically active substance can be removed.Type: GrantFiled: January 14, 1991Date of Patent: December 22, 1992Assignee: Japan Chemical Research Co., Ltd.Inventors: Hajime Hiratani, Jun Tateishi, Tetsuyuki Kitamoto
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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: 5134065Abstract: A novel and unique plasminogen activator inhibitor fragment is obtained from human umbilical vein endothelial cells which has the following characteristics:A. it is derived from a native t-PA inhibitor that binds to and inhibits the activity of t-PA,B. it is dissociated from a complex formed between said native t-PA inhibitor and t-PA, said complex existing in two distinct interconvertible conformations with molecular weight of about 88 KDa and 105 KDa, respectively, and being partially reversible in the presence of fibrin,C. it has a molecular weight of about 40 KDa when dissociated from the complex, andD. it has a novel partial N-terminal amino acid sequence when dissociated from the complex.Type: GrantFiled: May 16, 1986Date of Patent: July 28, 1992Assignee: Monsanto CompanyInventors: Michael A. Sanzo, Arthur J. Wittwer, Jayne C. Marasa, Joseph Feder
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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: 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: 5102987Abstract: The .alpha.-chlorohydrin content of liquid hydrolysed protein obtained by acid hydrolysis with hydrochloric acid is reduced by adjusting the pH of the liquid hydrolysed protein to a pH of from 8 to 14 and holding the liquid for a time sufficient for the .alpha.-chlorohydrin content of the liquid hydrolysed protein to be reduced.Type: GrantFiled: October 14, 1988Date of Patent: April 7, 1992Assignee: Nestec S.A.Inventors: Paul E. Cornet, Rebecca S. So, John S. Tandy
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Patent number: 5102989Abstract: Recombinant hepatitis B virus surface proteins produced in recombinant host cells are rapidly and efficiently purified from either cell extracts in a high pH buffer, or from heated whole cells at neutral pH. The host cell extracts or whole cells are heat treated, cooled and in the case of high pH extract, the pH is reduced. The surface proteins are then absorbed onto wide pore silica followed by elution and concentration. This method eliminates the requisite introduction of protease inhibitors, stabilizes the surface protein and improves product yield.Type: GrantFiled: March 15, 1991Date of Patent: April 7, 1992Assignee: Merck & Co., Inc.Inventors: Robert D. Sitrin, Dennis J. Kubek
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Patent number: 5087449Abstract: The present invention relates to a method for purification of a bifidobacteria-proliferating substance which comprises treating the extract of soybean or its treated matters or soybean whey or treated solutions thereof with an ultrafiltration membrane, treating with activated carbon and then subjecting to an electrodialysis treatment. The present invention also relates to the thus obtained bifidobacteria-proliferating substance.Type: GrantFiled: June 14, 1990Date of Patent: February 11, 1992Assignee: Calpis Food Industry Co., Ltd.Inventors: Teruhisa Masai, Takanobu Shibuta, Yasuyuki Yoshida, Yohsuke Suzuki
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Patent number: 5084558Abstract: A blood substitute and plasma expander comprising a cross-linked, substantially endotoxin-free homoglobin solution and process for preparing same. The process comprises fractionating whole blood, separating out a stromal-free, sterile hemoglobin solution, chromatographically separating endotoxins from said hemoglobin solution and crosslinking the resulting endotoxin-free hemoglobin solution.Type: GrantFiled: November 10, 1987Date of Patent: January 28, 1992Assignee: Biopure CorporationInventors: Carl W. Rausch, Mario Feola
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Patent number: 5084561Abstract: A new method for the purification of a 168 kD protein from Mycoplasma pneumoniae using zwitterionic and non-ionic detergents.Type: GrantFiled: March 21, 1989Date of Patent: January 28, 1992Inventors: Wolfgang Bredt, Klemens Fuchte, Enno Jacobs
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Patent number: 5066491Abstract: Whey derived from ordinary milk includes a bottom fraction including lactose and minerals, a middle fraction including lower molecular weight proteins, and a top fraction including higher molecular weight proteins. The top whey fraction includes a measurable but low level concentration of immunologically active immunoglobulin plus other pathogen specific antibodies. The whey is ultrafiltered through one or more different process steps to yield a filtered product having a concentration of immunologically active immunoglobulin of at least about seven percent of total solids. The filtered product is periodically tested to verify its activity to a specified microbe. The filtered product is orally administered in a therapeutically effective dose to an animal to treat a disease.Type: GrantFiled: February 3, 1989Date of Patent: November 19, 1991Assignee: Protein Technology, Inc.Inventors: Gerald H. Stott, David O. Lucas
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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: 5039794Abstract: A novel cell scattering factor, i.e., tumor egress factor (hereinafter "egressin") isolated from a clone derived from a human metastatic melanoma (M3827) which possesses a loose colony morphology and from a human monocytic cell line (U937) and processes for producing the same. Egressin is useful for the production of immunological reagents for the detection and treatment of metastatic lesions, for aiding in the transport of drugs across the blood-brain barrier, and for aiding in the control of the inflammatory response.Type: GrantFiled: September 15, 1987Date of Patent: August 13, 1991Assignee: Otsuka Pharmaceutical Co., Ltd.Inventors: Marjorie L. Wier, Joseph E. De Larco
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Patent number: 5039609Abstract: This invention relates to a peritoneal dialysis solution which comprises as an osmotically active agent an osmotically effective amount of a mixture of peptides, the mixture consisting substantially of peptides having a molecular weight of about 300 to about 2000 daltons, and an equivalent weight between about 150 to about 1500.Type: GrantFiled: April 18, 1988Date of Patent: August 13, 1991Assignee: Research Technologies, Inc.Inventor: Elias Klein
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Patent number: 5026828Abstract: Recombinant hepatitis B antigen bound to yeast membranes in yeast expression systems is rapidly purified by subjecting the membrane bound protein to agents that release undesired proteins, followed by agents that release the recombinant hepatitis B antigen.Type: GrantFiled: December 1, 1988Date of Patent: June 25, 1991Assignee: Merck & Co., Inc.Inventor: Shigeko Yamazaki
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Patent number: 5011915Abstract: Methods of purifying recombinant surface antigen of hepatitis B virus are disclosed. In one protocol, purification is achieved by selective extraction of the antigen from yeast membranes, followed by solubilization with urea and dithiothreitol.Type: GrantFiled: October 26, 1987Date of Patent: April 30, 1991Assignee: Merck & Co., Inc.Inventor: Shigeko Yamazaki