Proteinaceous Material Recovered Or Purified Patents (Class 435/272)
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Patent number: 4468457Abstract: A tryptic peptide is produced by partial tryptic digestion of purified, high molecular size colon-specific antigen-p (CSAp), to produce a lower molecular size antigen carrying the CSAp antigenic determinant. The tryptic peptide is used to produce monospecific anti-CSAp antibodies.Type: GrantFiled: June 1, 1981Date of Patent: August 28, 1984Assignee: David M. GoldenbergInventors: Milton D. Goldenberg, Dan Shochat
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Patent number: 4443540Abstract: The present invention prepares protein hydrolyzates by reacting selected protein material with at least one proteolytic enzyme and recovering the low molecular weight protein material by ultrafiltration while recycling the high molecular weight material and proteolytic enzyme for further hydrolysis. A series of ultrafilters of varying permeability may also be used.Type: GrantFiled: September 20, 1982Date of Patent: April 17, 1984Assignee: University of Illinois FoundationInventors: Munir Chervan, William D. Deeslie
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Patent number: 4436724Abstract: A method of producing .gamma.-globulin which can be administered intravenously without adverse reactions and loss of opsonic activity is provided. The method comprises treating .gamma.-globulin with pepsin or uropepsin in a neutral pH range of 6.0 to 7.5. The aggregates in .gamma.-globulin are selectively decomposed by the method of the present invention, while any decomposition of monomer .gamma.-globulin molecule is substantially prevented. A therapeutic agent for intravenous injection which is reduced its anticomplementary activity and is stabilized by adding uropepsin which serves simultaneously as a proteolytic enzyme and a stabilizer, to human .gamma.-globulin. Uropepsinogen can be also as a stabilizer.Type: GrantFiled: May 26, 1982Date of Patent: March 13, 1984Assignee: Mochida Pharmaceutical Co., Ltd.Inventors: Haruo Ohnishi, Hiroshi Kosuzume, Yasuo Suzuki, Ei Mochida
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Patent number: 4410660Abstract: A method for detecting the presence of Mycobacteria in a fluid or tissue which comprises mixing the fluid or tissue containing a secretory product of Mycobacteria with a complex of a tracer-containing molecule and a binding macromolecule having reversible binding affinity for the tracer-containing molecule and detecting the tracer-containing molecule, wherein the tracer-containing molecule is a charcoal-adsorbable protein from Mycobacterium tuberculosis which has a molecular weight of 20,000-30,000 and which is immunochemically stable from 4.degree.0 C. to 250.degree. C. and has a pH range from 3.0 to 9.0. The method is particularly applicable to the detection of infectious tuberculosis in humans and determining the antibiotic sensitivity of infecting Mycobacteria.Type: GrantFiled: May 5, 1980Date of Patent: October 18, 1983Assignee: Montefiore Medical CenterInventor: Eugene W. Straus
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Patent number: 4399123Abstract: A fibrous tissue preparation suitable for homo or heterotransplantation is obtained by treating mammalian fibrous tissue with a proteolytic enzyme followed, if desired, by further treatment with a carbohydrate splitting enzyme.Type: GrantFiled: December 29, 1980Date of Patent: August 16, 1983Inventors: Roy F. Oliver, Roy A. Grant
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Patent number: 4377514Abstract: A process for making factor for stimulating the rate of proliferation of liver cells comprising homogenizing animal Peyer's glands, adjusting pH to about 5.5, thermally denaturing the product and recovering the desired factor in the supernatant by centrifugation.Type: GrantFiled: October 5, 1981Date of Patent: March 22, 1983Assignee: Max-Planck-Gesellschaft zur Foerderung der Wissenschaften E.V.Inventors: Gerhard Ruhenstroth-Bauer, Michel Goldberg, Hubertus Schneider
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Patent number: 4370267Abstract: The 7S and 11S proteins of vegetable proteins may be effectively fractionated and isolated by selectively extracting 7S proteins from an isoelectrically precipitated mixture of 7S and 11S protein in the presence of water-soluble salts. The initial 7S extraction is typically conducted at a pH 5.0-5.6. An enriched 11S fraction is recovered by separating the water-insoluble 11S protein from the water-soluble enriched 7S extract.Type: GrantFiled: August 10, 1981Date of Patent: January 25, 1983Assignee: A. E. Staley Manufacturing CompanyInventors: William F. Lehnhardt, Paul W. Gibson, Frank T. Orthoefer
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Patent number: 4361587Abstract: Phosphopeptides useful as dietetic aliments, therapeutic nutriments or medicaments are produced by subjecting phosphocaseinates of bivalent cations to enzymatic hydrolysis with at least one proteolytic enzyme capable of substantially reproducing the proteic digestion which occurs in vivo in the human body to produce a hydrolysate containing phosphopeptides and non-phosphorylated peptides, subjecting the resultant hydrolysate to ultrafiltration to obtain a retentate containing the phosphopeptides and proteolytic enzyme and a permeate containing the non-phosphorylated peptides, disaggregating the phosphopeptides in the retentate and subjecting the resultant retentate containing disaggregated phosphopeptides to ultrafiltration to separate the phosphopeptides from the proteolytic enzyme. Salts of the phosphopeptides, which have dietetic uses, may be formed from macroelements such as calcium and/or magnesium and/or from oligoelements such as iron, zinc and copper.Type: GrantFiled: January 28, 1981Date of Patent: November 30, 1982Assignee: Institut National de la Recherche AgronomiqueInventors: Gerard Brule, Loic Roger, Jacques Fauquant, Michel Piot
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Patent number: 4359532Abstract: An improved method suitable for extracting glucose from green crops, such as leaves, grasses, legumes, stems of green plants and tree leaves. The method comprises the steps of subjecting the green crops to a pulping action in an organic acid solution recirculated from a subsequent fermentation separation step to produce a pulp comprising a protein-rich liquid and fibrous material, separating protein-rich liquid in the pulp from the fibrous material and separating protein from the protein-rich liquid by initiating anaerobic fermentation in an acidic solution thereby providing a concentrated protein fraction suitable for preservation and an acidic solution. At least a portion of the acidic solution is recycled to the separation step, the recycling of the solution being provided for purposes of washing the fibrous material to remove residual protein therefrom.Type: GrantFiled: September 8, 1980Date of Patent: November 16, 1982Assignee: Aluminum Company of AmericaInventor: Melvin H. Brown
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Patent number: 4359530Abstract: A method of extracting protein from green crops such as leaves, grasses, legumes, stems of green plants and tree leaves is disclosed. The method comprises the steps of subjecting the green crops to a pulping action in an acid solution recirculated from a subsequent anaerobic fermentation step to produce a pulp comprising a protein-rich liquid and fibrous material. The protein-rich liquid in the pulp is separated from the fibrous material. The protein is separated from the protein-rich liquid by anaerobic fermentation in an acidic solution thereby providing a concentrated protein fraction suitable for preservation and an acidic solution at least a portion of which is recycled to insure further removal of protein from the fibrous material.Type: GrantFiled: September 8, 1980Date of Patent: November 16, 1982Assignee: Aluminum Company of AmericaInventor: Melvin H. Brown
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Patent number: 4358465Abstract: Phosphopeptides useful as alimentary products or as medicaments are obtained by a method of subjecting phosphocaseinates of monovalent cations or paracasein derived therefrom to enzymatic hydrolysis with at least one proteolytic enzyme that simulates proteic digestion in vivo in the human body, ultrafiltering the resultant hydrolysate with a membrane that retains the enzyme to obtain a permeate containing phosphopeptides and non-phosphorylated peptides, adding to the permeate a bivalent cation salt to form aggregates of the phosphopeptides, subjecting the resultant solution to ultrafiltration with a membrane that retains the phosphopeiptide aggregates, and recovering the retained phosphopeptides. The phosphopeptides form salts, which have dietetic uses, with macroelements such as calcium and/or magnesium and/or oligoelements such as iron and zinc.Type: GrantFiled: January 28, 1981Date of Patent: November 9, 1982Assignee: Institut National de la Recherche AgronomioueInventors: Gerard Brule, Loic Roger, Jacques Fauquant, Michel Piot
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Patent number: 4330623Abstract: Gonococcal antigens are solubilized by a process involving trypsin-digestion.Type: GrantFiled: February 19, 1980Date of Patent: May 18, 1982Assignee: Merck & Co., Inc.Inventor: Yashwant D. Karkhanis
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Patent number: 4330560Abstract: The process consists of cultivating, at a temperature below 28.degree. C., the fungus Trichoderma Album in liquid nutrient media, the pH of said media being kept at a value comprised between about 3.7 and 4.8, the dissolved oxygen content being from about 6 to 10 mg/l. The cultivation is carried out with non-traumatizing, efficient stirring and under conditions such that multiplication is practically nil.Type: GrantFiled: July 7, 1980Date of Patent: May 18, 1982Assignee: Institut National de la Recherche AgronomiqueInventor: Thadee J. Staron
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Patent number: 4319885Abstract: A method of reducing sulfurous pollutants from furnaces fired with sulfur-containing coals is disclosed. The method comprises the steps of recovering fibrous material from green crops, comprising leaves, grasses, legumes, stems of green plants and tree leaves by subjecting the green crops to a mechanical pulping action and separating juices generated by the pulping action from the fibrous material. The fibrous materials are burned with the sulfur-containing coal in the furnace thereby permitting alkaline residues from the fibrous material to react with sulfur oxides generated by the combustion of the coal, the reaction converting the oxides to sulfur salts and permitting the salts to be recovered in ash from the furnace thereby reducing the pollutants from the furnace by the reaction and by dilution of the combustion gases.Type: GrantFiled: September 8, 1980Date of Patent: March 16, 1982Assignee: Aluminum Company of AmericaInventor: Melvin H. Brown
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Patent number: 4313962Abstract: Casein having a reduced cholesterol content is obtained by treating skimmilk at a pH of about 6.0 to 6.9 with a pancreatic lipase having lipase activity and protease activity for a time sufficient to dissociate the casein from cholesterol therein and then coagulating the casein by enzymatic means.Type: GrantFiled: April 16, 1980Date of Patent: February 2, 1982Assignee: Miles Laboratories, Inc.Inventors: Chong Y. Kim, Moshe M. Sternberg
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Patent number: 4312949Abstract: A gamma globulin solution suitable for intravenous use is prepared by treating the gamma globulin fraction of plasma or serum obtained in known manner with a peptic enzyme at a pH value of about 4. The treatment is carried out with at most 20,000 A.E./100 g. protein at a temperature of about from 37.degree.-40.degree. C.Type: GrantFiled: February 2, 1981Date of Patent: January 26, 1982Assignee: Blutspendedienst det Landesverbande des Deutschen Roten Kreuzes Niedersachsen, Oldenburg und Bremen GmbHInventor: Ulrich E. Ahrens
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Patent number: 4288557Abstract: An antigenic, immunogenic, non-toxic complex is obtained from the cell surface of N. gonorrhoeae.Type: GrantFiled: March 5, 1980Date of Patent: September 8, 1981Assignee: Merck & Co., Inc.Inventors: Yashwant D. Karkhanis, Dennis J. Carlo
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Patent number: 4285976Abstract: Autolysis of yeast slurries is accelerated by the presence of thiamine and/or pyridoxine and by gradually raising the temperature of the yeast slurry to the incubation temperature over a period of time of from about 20 to about 180 minutes.Type: GrantFiled: November 23, 1979Date of Patent: August 25, 1981Assignee: Standard Oil Company (Indiana)Inventors: Cavit Akin, Rose M. Murphy
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Patent number: 4279996Abstract: Water-soluble keratin hydrolyzate having at least two mercapto groups in one molecule and having an average molecular weight of 2,000 to 20,000, suitable for cosmetic application to the hair, particularly as hair fixatives. The hydrolyzate is prepared by reducing keratin in an aqueous solution of a reducing agent under alkaline conditions and subjecting the resulting reduction product to enzymatic hydrolysis.Type: GrantFiled: September 25, 1979Date of Patent: July 21, 1981Assignee: Seiwa Kasei Co., Ltd.Inventors: Issei Yoshioka, Yoichi Kamimura
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Patent number: 4277250Abstract: A method for detecting occult blood in aqueous samples of human specimens, particularly aqueous suspensions of fecal matter is disclosed. The method comprises acidifying an aqueous test sample, which in the case of fecal matter has been treated with lysozyme to clear the suspension; separating the liquid and solid portions of the test sample and passing the acidified liquid portion through an electro-negatively charged membrane; thereafter removing residual test liquids from the membrane; treating the membrane with a peroxidase indicator and observing the development of color on the treated membrane surface. A method for quantifying occult blood is also disclosed which comprises subjecting an aqueous sample to the disclosed detection method and comparing the color developed with a standardized scale reflecting colors developed by treating samples containing known incremental quantities of hemoglobin in accordance with the detection method of the invention.Type: GrantFiled: December 10, 1979Date of Patent: July 7, 1981Assignee: Baylor College of MedicineInventors: Joseph L. Melnick, Craig Wallis
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Patent number: 4267275Abstract: A method of recovering water-insoluble and water-soluble protein fractions from protein-polysaccharide complexes such as wheat gluten involves subjecting a complex of this type to an enzyme treatment in the presence of a liquid so as to decompose at least a portion of the polysaccharide content of the complex and dissolve at least a portion of the protein content of the complex thereby obtaining a suspension of protein solids in the solution formed by the liquid. The liquid used is preferably water. The suspension is separated into a solids fraction and a liquid fraction by centrifugation of filtration. The solids fraction and liquid fraction are then treated separately from one another to thereby obtain a water-insoluble protein fraction and a water-soluble protein fraction. The treatment of the solids fraction may involve washing of the same followed by drying.Type: GrantFiled: October 18, 1978Date of Patent: May 12, 1981Assignee: Dr. Ing Hans MullerInventor: Hans Muller
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Patent number: 4250265Abstract: A sub-cellular antigenic fraction of Bordetella bronchiseptica protects against the incidence and severity of swine atropic rhinitis.Type: GrantFiled: October 15, 1979Date of Patent: February 10, 1981Assignee: Merck & Co., Inc.Inventors: Dennis J. Carlo, Arpi Hagopian, Peter J. Kniskern
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Patent number: 4242326Abstract: An anti-tumor substance which is not only heatstable but also has low inflaming and pain-inducing properties and low pyrogenic activity is disclosed. The substance is prepared by disrupting cells of bacteria belonging to hemolytic streptococci, extracting from the disrupted material a water-insoluble substance and treating the substance with one or more proteases and, optionally, with one or more nucleases.Type: GrantFiled: June 18, 1979Date of Patent: December 30, 1980Assignee: Chugai Seiyaku Kabushiki KaishaInventors: Yutaka Sugawara, Akihiro Yamamoto, Mitsuaki Handa, Hiroko Usami, Haruki Ogawa
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Patent number: 4233406Abstract: A process for the enzymatic streatment of waste water of wheat starch plants in which the waste water is subjected before or alternating with the first steps of the concentration process to a process at least consisting of(a) a heat treatment followed by separation of the solid substance, and(b) a treatment with enzyme preparations exhibiting amylase and/or cellulase and/or hemi-cellulase activity and optionally glucoamylase and/or .beta.-glucanase activity.Type: GrantFiled: October 13, 1978Date of Patent: November 11, 1980Assignees: Naarden International N.V., Altenburger Maschinen KG Jaeckering & Co.Inventors: Andras J. Wieg, Gunther Jackering
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Patent number: 4232044Abstract: Food protein flavor is improved by enzymatic conversion of the aldehydes and alcohols in such protein.Type: GrantFiled: August 21, 1978Date of Patent: November 4, 1980Assignee: Kyowa Hakko Kogyo Co., Ltd.Inventors: Hideo Chiba, Ryuzo Sasaki, Masaaki Yoshikawa, Naofumi Takahashi, Etsuro Sugimoto, Hirotoshi Samejima
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Patent number: 4232123Abstract: A method is disclosed for making a water-soluble hydrolyzate of a keratinaceous starting material which comprises first subjecting said starting material to acid treatment at a pH of 2 or below and at an elevated temperature above 80.degree. C. to effect mild hydrolysis thereof and then enzymatically degrading said acid-treated material in an aqueous bath in the presence of urea with an alkaline proteinase having an activity optimum in a range between pH 9 and pH 13, the initial pH of the enzymatic treatment being within the pH range optimum for the enzyme employed.Type: GrantFiled: July 9, 1979Date of Patent: November 4, 1980Assignees: Firma Carl Freudenberg, R/hm GmbHInventors: Klaus Braeumer, Zdenek Eckmayer, Alexander Berg, Rolf Monsheimer, Ernst Pfleiderer
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Patent number: 4218481Abstract: Yeast autolysis is enhanced by the addition of certain exogenous enzymes to the yeast slurry at concentrations of from about 0.01-1.0 weight percent, said enzymes being selected from the group consisting of papain, ficin, bromelain, pancreatin, and aspergillus protease.Type: GrantFiled: October 6, 1978Date of Patent: August 19, 1980Assignee: Standard Oil Company (Indiana)Inventors: Kwei C. Chao, Edward F. McCarthy, George A. McConaghy
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Patent number: 4217414Abstract: A mixture of vital wheat gluten and starch containing at least 25% protein, e.g. a protein-rich fraction of wheat flour, is treated with a bacterial alpha-amylase (preferably substantially free of protease) under conditions which solubilize the starch but do not unduly solubilize, or denature, the vital gluten. Specifically, the temperature should be not above about 80.degree. C. and the time of treatment should not exceed about 6 hours. After the enzymatic treament the gluten, which still retains its vital properties, is separated out, and the solubilized starch fraction is recovered or subjected to further processing.Type: GrantFiled: July 10, 1978Date of Patent: August 12, 1980Assignee: CPC International Inc.Inventor: Raoul G. P. Walon
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Patent number: 4184917Abstract: The invention provides structurally modified interferons, processes for producing such and a method of purification of interferons and structurally modified interferons. The modified interferons are useful as anti-viral agents.Type: GrantFiled: September 19, 1977Date of Patent: January 22, 1980Assignee: Sandoz Ltd.Inventors: Friedrich Dorner, Marianne Scriba, Rudolf Weil
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Patent number: 4182654Abstract: A process is disclosed for synthesizing a peptide chain involving reacting, in aqueous solution, an amino acid containing a blocked alpha amino or carboxyl group with a polynucleotide handle to form a covalently bonded complex. The complex is separated from unreacted acid by reversible coupling to a complementary polynucleotide adsorbent immobilized on an insoluble support, and then the complex is eluted from the support as an aqueous solution. The complex is then enzymatically deblocked and used as the precursor for repeating the reaction with a further acid and the process reiterated. During the process, those chains which failed to react with a given acid can be removed by enzymatic degradation.Type: GrantFiled: May 19, 1978Date of Patent: January 8, 1980Assignee: Pierce Chemical CompanyInventor: Garfield P. Royer
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Patent number: 4180627Abstract: Precipitates soluble in aqueous solution and suitable for stimulation and/or transfer of cell-mediated immunity in mammals and other animals is disclosed together with a solvent extraction process for obtaining this desirable product from crude bovine transfer factor. Lymphocytes from lymph nodes and blood of donor cattle are employed in formulating a Bovine Transfer factor by incubation release procedure. The fractionation of Bovine Transfer factor yields three precipitate fractions by the use of organic solvents. A relatively high incidence of transfer with the precipitates yields excellent immunity to certain diseases in animals.Type: GrantFiled: August 17, 1978Date of Patent: December 25, 1979Assignee: The United States of America as represented by the Secretary of AgricultureInventors: Phillip H. Klesius, Herman H. Fudenberg
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Patent number: 4172072Abstract: Protein sources are subjected to hydrolysis by the action of specific proteases under neutral conditions and are then reacted with water soluble bivalent metal salts in an aqueous alkaline media to form metal proteinates which are then buffered thereby forming biologically acceptable metal proteinates which are protected from adverse acid or alkaline destruction.Type: GrantFiled: October 20, 1977Date of Patent: October 23, 1979Inventor: Harvey H. Ashmead
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Patent number: RE31517Abstract: A method for the quantitative determination of renin activity in blood utilizing the measurement of Angiotensin I by treating the blood with ethylenediaminetetraacetic acid (EDTA) and the plasma with phenylmethyl sulfonylfluoride (PMSF) at a preferred pH to ascertain the full range of concentration where PMSF is effective for accurate and quick determination.Also, a method for the quantitative determination of renin activity in blood utilizing the measurement of Angiotensin I by incubating the samples after antibody addition at room temperature (23.degree. to 30.degree. C.) for 1 to 2 hours and separating the free from the antibody bound species with polyethylene glycol after having treated the blood with ethylenediaminetetraacetic acid (EDTA) and the plasma with phenylmethyl sulfonylfluoride (PMSF) at a preferred pH.Type: GrantFiled: September 15, 1978Date of Patent: February 7, 1984Inventor: Aurora L. Fernandez de Castro