Separation Or Purification Patents (Class 530/412)
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Patent number: 8809510Abstract: A method for purification of complement Factor H from a complement Factor H containing source such as blood or blood plasma, in particular a caprylate precipitate of a Factor H containing source, which is e.g. obtained by addition of caprylate ions to fractions of blood or plasma, comprising the steps of: a) providing a Factor H containing source, in particular reconstitution of caprylate precipitate to provide a complement Factor H containing solution; b) performing a cation exchange chromatography in particular as first chromatographic step; c) performing an anion exchange chromatography; d) performing a hydroxyl apatite chromatography; e) followed by ultra/diafiltration to obtain a complement Factor H concentrate.Type: GrantFiled: October 13, 2011Date of Patent: August 19, 2014Assignee: Octapharma AGInventors: Hubert Brandstaetter, Petra Schulz, Juergen Roemisch
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Patent number: 8809509Abstract: A method for manufacturing an antibody formulation in which DNA contaminants are removed by binding the antibody to a protein-A or probtin-G affinity column and eluting the antibody with an acidic eluting solution, preferably of low conductivity.Type: GrantFiled: March 20, 2013Date of Patent: August 19, 2014Assignee: Chugai Seiyaku Kabushiki KaishaInventors: Kozo Takeda, Norimichi Ochi, Kimie Ishii, Manabu Matsuhashi, Akinori Imamura
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Patent number: 8802828Abstract: Methods for refolding antibodies, particularly monoclonal antibodies, from aggregated and/or denatured preparations by subjecting the antibody preparation to high hydrostatic pressure are provided. Refolded preparations of antibodies produced by the methods described herein are also provided.Type: GrantFiled: February 27, 2012Date of Patent: August 12, 2014Assignee: Barofold, Inc.Inventors: Matthew B. Seefeldt, Robert Nelson, Theodore W. Randolph, Lyndal K. Hesterberg
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Patent number: 8796430Abstract: The present invention provides improved methods for the manufacturing of IVIG products. These methods offer various advantages such as reduced loss of IgG during purification and improved quality of final products. In other aspects, the present invention provides aqueous and pharmaceutical compositions suitable for intravenous, subcutaneous, and/or intramuscular administration. In yet other embodiments, the present invention provides methods of treating a disease or condition comprising administration of an IgG composition provided herein.Type: GrantFiled: April 12, 2011Date of Patent: August 5, 2014Assignees: Baxter International Inc., Baxter Healthcare SAInventors: Leopold Bruckschwaiger, Sonja Svatos, Julia Nürnberger, Wolfgang Teschner, Harald Arno Butterweck, Hans-Peter Schwarz, Thomas Gundinger, Bernhard Koelbl, Reinhard Grausenburger, Azra Pljevljakovic
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Publication number: 20140212885Abstract: The application provides a method of reducing the DNA content of a protein preparation or a culture broth from a filamentous fungal host cell using an endogenous filamentous fungal host DNase activity.Type: ApplicationFiled: September 20, 2012Publication date: July 31, 2014Applicant: Danisco US Inc.Inventors: Katherine M. Hoffmann, Douglas Ko, Michael Ward
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Patent number: 8772461Abstract: The present invention provides a method for concentrating a protein, in particular a method for concentrating a plasma product, in particular IgG, using glycine in a (two-stage ultrafiltration/diafiltration approach.Type: GrantFiled: April 14, 2009Date of Patent: July 8, 2014Assignee: Grifols Therapeutics Inc.Inventors: Martin Gonzalez, Woody D. Wood, Fred H. Earp
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Patent number: 8772018Abstract: The invention relates generally to solid supports for chromatography. In specific embodiments the invention provides for solid supports suitable for affinity chromatography along with methods, systems and kits which use the same.Type: GrantFiled: July 7, 2008Date of Patent: July 8, 2014Assignee: EMD Millipore CorporationInventors: Nanying Bian, Senthil Ramaswamy, Neil Soice, Chen Wang, Yuan Wong
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Patent number: 8765922Abstract: A method and associated device for enrichment of Neél-magnetic particles from a dispersion of Brown-magnetic particles and Neél-magnetic particles. The device and method use ferromagnetic separation particles having a mean diameter of 100 to 250 ?m located in a alternating magnetic field. The ferromagnetic separation particles have a magnetically and chemically inert coating.Type: GrantFiled: October 19, 2011Date of Patent: July 1, 2014Assignee: Miltenyi Biotec GmbHInventors: Jürgen Schulz, Daniel Michalek, Dirk Merkel, Stefan Miltenyi
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Patent number: 8765923Abstract: Methods for selective extraction and fractionation of algal proteins from an algal biomass or algal culture are disclosed. A method of selective removal of products from an algal biomass provides for single and multistep extraction processes which allow for efficient separation of algal proteins. These proteins can be used as renewable sources of proteins for animal feedstocks and human food. Further, lipids remaining in the algal biomass after extraction of proteins can be used to generate renewable fuels.Type: GrantFiled: December 20, 2011Date of Patent: July 1, 2014Assignee: Heliae Development, LLCInventor: Aniket Kale
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Patent number: 8765411Abstract: The subject invention provides an improved process for the production of human growth hormone.Type: GrantFiled: September 20, 2011Date of Patent: July 1, 2014Assignee: Ferring B.V.Inventors: Dov Kanner, Eli Schmell
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Patent number: 8759027Abstract: The expression vectors and methods using an E. coli expression system for the large scale production of IL-29 are described. The vectors utilize the IL-29 coding sequence with specific changes in nucleotides in order to optimize codons and mRNA secondary structure for translation in E. coli. Also included are methods of producing, purifying and pegylating an IL-29 polypeptide.Type: GrantFiled: December 19, 2012Date of Patent: June 24, 2014Assignee: ZymoGenetics, Inc.Inventors: Bruce L. Zamost, Geoffrey F. Lee, Robert M. Dedinsky
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Patent number: 8754196Abstract: The present invention relates to chromatography matrices including ligands based on one or more domains of immunoglobulin-binding proteins such as, Staphylococcus aureus Protein A (SpA), as well as methods of using the same.Type: GrantFiled: June 6, 2012Date of Patent: June 17, 2014Assignee: EMD Millipore CorporationInventors: Shari Spector, Robert Smith, Joe Orlando, Nanying Bian
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Patent number: 8754168Abstract: A method is provided for solubilising a membrane protein. The method is applied to cellular material comprising the membrane protein and an associated membrane lipid. A copolymer of styrene and maleic acid, wherein the styrene:maleic acid ratio is between 1:2 and 10:1, is mixed with the cellular material to cause the copolymer, lipid and protein to form soluble macromolecular assemblies.Type: GrantFiled: July 8, 2010Date of Patent: June 17, 2014Assignee: The University of BirminghamInventors: Timothy Dafforn, Michael Overduin, Timothy Knowles
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Patent number: 8748588Abstract: Methods for selective extraction and fractionation of algal proteins from an algal biomass or algal culture are disclosed. A method of selective removal of products from an algal biomass provides for single and multistep extraction processes which allow for efficient separation of algal proteins. These proteins can be used as renewable sources of proteins for animal feedstocks and human food. Further, lipids remaining in the algal biomass after extraction of proteins can be used to generate renewable fuels.Type: GrantFiled: October 7, 2011Date of Patent: June 10, 2014Assignee: Heliae Development, LLCInventor: Aniket Kale
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Patent number: 8741629Abstract: Methods for selective extraction and fractionation of algal proteins from an algal biomass or algal culture are disclosed. A method of selective removal of products from an algal biomass provides for single and multistep extraction processes which allow for efficient separation of algal proteins. These proteins can be used as renewable sources of proteins for animal feedstocks and human food. Further, lipids remaining in the algal biomass after extraction of proteins can be used to generate renewable fuels.Type: GrantFiled: November 4, 2011Date of Patent: June 3, 2014Assignee: Heliae Development, LLCInventor: Aniket Kale
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Publication number: 20140147904Abstract: The present invention relates to a filtering apparatus and method for mixing a compound of solid and fluid phases, separating the phases and/or extracting fluid from the compound. One embodiment of the invention discloses a filtering apparatus comprising a first filter section accommodating a first group of filter members, and a second filter section accommodating a second group of filter members, a piping system providing pipelined fluid communication between the filter sections and between a filter section and said filter section's corresponding group of filter members, the piping system configured such that the filter members form filtered fluid openings of the filtering apparatus, and circulation means, such as a pump, configured for passing fluid in a forward flow and/or in a reverse flow between the filter sections. In particular the invention may be used for the mashing process in a beer brewing procedure.Type: ApplicationFiled: August 13, 2012Publication date: May 29, 2014Applicant: TECHNICAL UNIVERSITY OF DENMARKInventors: Peter Stubbe, Preben Bøje Hansen
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Patent number: 8734854Abstract: A sub-atmospheric, negative pressure is applied to a growth factor starting material, such as whole blood, to release growth factors and plasma in a non-destructive medium. The released growth factors having a weight of about 70-76 kDaltons are applied in either a filtered or unfiltered state to a wound to promote healing of the wound. The released growth factors are applied topically to the area of a surface wound to effect healing. The released growth factors are also injected into soft tissue, such as a torn tendon, to promote tissue growth and healing. The growth factors are released in one method from a patient's own blood. In another method the growth factors are released from a whole blood source and freeze dried by conventional lyophilization. Then at a later date, the freeze dried product is reconstituted by normal saline for treatment of a patient's wound or for use in a surgical procedure.Type: GrantFiled: July 9, 2009Date of Patent: May 27, 2014Inventors: James B. Gandy, Robert J. Brandt, Ryan N. Brandt, Clark Galen, Joseph F. Greco, John Kiwczak
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Patent number: 8735122Abstract: Recombinant purified DnaK—having a ATPase activity without the addition of an other chaperone protein—essentially free of T-cell stimulating impurities.Type: GrantFiled: October 12, 2007Date of Patent: May 27, 2014Assignee: Biotech Tools S.A.Inventors: Frederic Henot, Thierry Legon, Sabine Pirotton, Gael Placier
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Patent number: 8735544Abstract: An improved process for obtaining value added by-products from an ethanol production whole stillage is disclosed wherein the whole stillage is mixed with additives to form a nutrition enriched product stream that is subsequently dried to produce a nutrition enriched product having a water content of less than 12% by weight. In a preferred embodiment the whole stillage is obtained from a ethanol production process that has utilized a corn flour as the starting feedstock. The corn flour is then hydrolyzed along with added vitamins and/or nutrients and/or enzymes. The hydrolyzed product is then preferably mixed with a soy hull flour, also preferably having a median particle size of less than about 100 microns, and subjected to conventional fermentation conditions to produce an ethanol containing product. The ethanol-containing product is then distilled to produce an ethanol enriched steam and the separate whole stillage to be used as the feedstock.Type: GrantFiled: September 28, 2005Date of Patent: May 27, 2014Assignee: Little Sioux Corn Processors, LLCInventors: John E. Prevost, Neal A. Hammond
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Publication number: 20140141446Abstract: The invention relates to an aptamer that binds to protein A, G or L, protein A-, G- or L-containing substances, and also to protein A-, G- or L-containing microorganisms, in particular Staphylococcus aureus, Streptococcus or Peptostreptococcus, methods for detection and enrichment of protein A, G or L, protein A-, G- or L-containing substances or protein A-, G- or L-containing microorganisms in which the aptamer is used, and also a kit, a biosensor, a lateral flow assay device and a measuring instrument which contain such an aptamer and can be used in said methods.Type: ApplicationFiled: March 29, 2012Publication date: May 22, 2014Applicant: Helholtz-Zentrum für Umweltforschung GmbH-UFZInventors: Regina Stoltenburg, Beate Strehlitz
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Patent number: 8729244Abstract: The invention relates to a method for purifying factor B, comprising the steps consisting in: (i) obtaining a blood plasma fraction containing factor B; (ii) subjecting the fraction obtained in step (i) to a heparin-like affinity chromatography; (iii) subjecting the factor B-enriched fraction obtained in step (ii) to a cation exchange chromatography; (iv) subjecting the factor B-enriched fraction obtained in step (iii) to an anion exchange chromatography, (v) eluting the factor B.Type: GrantFiled: November 15, 2010Date of Patent: May 20, 2014Assignee: Laboratoire Francais du Fractionnement et des BiotechnologiesInventor: Michel Poulle
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Patent number: 8729235Abstract: The invention provides an isolated major ampullate spidroin protein, which consists of from 150 to 420 amino acid residues and is defined by the formula REP-CT. REP is a repetitive, N-terminally derived protein fragment having from 80 to 300 amino acid residues. CT is a C-terminally derived protein fragment having from 70 to 120 amino acid residues. The invention further provides an isolated fusion protein consisting of a first protein fragment, which is a major ampullate spidroin protein, and a second protein fragment comprising a fusion partner and a cleavage agent recognition site. The first protein fragment is coupled via said cleavage agent recognition site to the fusion partner. The invention also provides a method of producing a major ampullate spidroin protein and polymers thereof.Type: GrantFiled: November 21, 2013Date of Patent: May 20, 2014Assignee: Spiber Technologies ABInventors: Jan Johansson, Gäran Hjäm, Margareta Stark, Anna Rising, Stefan Grip, Wilhelm Engsträm, My Hedhammar
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Patent number: 8729233Abstract: A nanowire comprising a purified protein filament, such as a pilus, isolated from a bacterium, such as Geobacter sulfurreducens, is provided. Such a purified pilus can contain peptide subunits capable of assembling into the protein filament and establishing an electrical connection with an insoluble electron acceptor. The novel nanowires can be produced via a novel single step. Such nanowires are useful in applications requiring rectifying behavior.Type: GrantFiled: August 30, 2011Date of Patent: May 20, 2014Assignee: Board of Trustees of Michigan State UniversityInventors: Gemma Reguera, Stuart Tessmer, Joshua Veazey, Sanela Lampa-Pastirk
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Patent number: 8710197Abstract: The present disclosure provides an effective method for the refolding of denatured proteins in solution so that properly folded, biologically active protein in solution is recovered in high yield. The refolding takes place at pressures between about 0.25 kbar to about 3.5 kbar, advantageously at about 1.5 kbar to about 3 kbar. Typically a chaotropic agent is present at a concentration which is not effective for denaturing protein at atmospheric pressure, and optionally, oxidation-reduction reagents can be incorporated in the refolding solution so that native intramolecular disulfide bonds can be formed where that is desired. The method is applicable to substantially all proteins, especially after solubilization and/or denaturation of insoluble protein aggregates, inclusion bodies, or abnormal oligomeric (soluble) aggregates.Type: GrantFiled: November 5, 2010Date of Patent: April 29, 2014Assignee: Barofold, Inc.Inventors: Theodore W. Randolph, John F. Carpenter, Richard St. John
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Patent number: 8709818Abstract: The invention provides methods of preparation of lipoproteins from a biological sample, including HDL, LDL, Lp(a), IDL, and VLDL, for diagnostic purposes utilizing differential charged particle mobility analysis methods. Further provided are methods for analyzing the size distribution of lipoproteins by differential charged particle mobility, which lipoproteins are prepared by methods of the invention. Further provided are methods for assessing lipid-related health risk, cardiovascular condition, risk of cardiovascular disease, and responsiveness to a therapeutic intervention, which methods utilize lipoprotein size distributions determined by methods of the invention.Type: GrantFiled: August 20, 2012Date of Patent: April 29, 2014Assignee: Quest Diagnostics Investments IncorporatedInventors: Michael P. Caulfield, Richard E. Reitz, Shuguang Li, Gloria Kwangja Lee, Ronald Krauss, Patricia J. Blanche, W. Henry Benner, Earl Cornell
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Patent number: 8710196Abstract: A method for purifying a polypeptide by ion exchange chromatography is described in which a gradient wash is used to resolve a polypeptide of interest from one or more contaminants.Type: GrantFiled: October 4, 2011Date of Patent: April 29, 2014Assignee: Genentech, Inc.Inventors: Jefferson C. Emery, Paul J. McDonald, Rhona O'Leary
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Patent number: 8703903Abstract: The invention relates to method for quantification of the absolute amount of allergen in an allergen sample comprising: a) providing a known amount of one or more allergen calibration standard peptide(s) having a sequence of amino acids which is identical with, and optionally unique for, a sequence to be found in the allergen to be quantified and optionally labelling said allergen calibration standard peptide(s), b) degrading the allergen sample to obtain a mixture of peptides, and optionally labelling said peptides with one or more labelling agent(s), wherein at least the peptides in the degraded allergen sample or the calibration standard peptides are labelled, and if both the peptides in the degraded allergen sample and the allergen calibration standard peptide(s) are labelled, the labelling agent(s) used for labelling the allergen calibration standard peptide(s) are different from the labelling agent(s) used for labelling the peptides of the degraded allergen sample, c) quantifying the absolute amount ofType: GrantFiled: September 1, 2006Date of Patent: April 22, 2014Assignee: ALK-Abello A/SInventor: Ulla Seppala
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Patent number: 8703706Abstract: The present invention relates to a closed container holding a composition of an activated Factor VII polypeptide in an amount of in the range of 2.5-90 mg per imL volume of the container. The invention also relates to various processes for the preparation of such closed containers, a kit including such containers and a method of using the kit.Type: GrantFiled: April 28, 2006Date of Patent: April 22, 2014Assignee: Novo Nordisk Healthcare AGInventors: Anne Charlotte Arentsen, Per Kaersgaard
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Patent number: 8697847Abstract: The present invention provides methods for purifying proteins. In particular, the methods employ a two-step non-affinity chromatography process without the use of an in-process tangential flow filtration step.Type: GrantFiled: March 2, 2012Date of Patent: April 15, 2014Assignee: Medarex, L.L.C.Inventors: Alahari Arunakumari, Gisela M. Ferreira
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Patent number: 8697844Abstract: The invention relates to a method of purifying PEGylated proteins by removing impurities from samples containing PEGylated proteins, in particular, but not exclusively vitamin K-dependent blood coagulation factors such as Factor IX (FIX), to proteins purified by said method and to the use of said purified proteins in therapy, in particular but not exclusively, for the treatment of diseases alleviated by blood coagulation factors such as the prophylactic treatment of hemophilia.Type: GrantFiled: November 24, 2010Date of Patent: April 15, 2014Assignee: Novo Nordisk A/SInventors: Matthias Karl Dietrich Wiendahl, Lars Sejersgaard, Are Bogsnes
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Patent number: 8680250Abstract: The present invention is one that, in a pollen protein extracting method, enables mass production, and while improving production efficiency, achieves a reduction in workload such as a reduction in man-hours, reductions in equipment cost and running cost, and an improvement of a work environment. Specifically, a pollen protein extracting method for extracting water-soluble protein from pollen is characterized by including: mixing the pollen and PBS; adding an aggregating agent including a natural inorganic component to a resultant mixed solution and performing stirring; and after formation of a pollen aggregate, performing filter filtration to perform solid-liquid separation.Type: GrantFiled: May 10, 2010Date of Patent: March 25, 2014Assignees: Wako Filter Technology Co., Ltd., Protec Co., Ltd.Inventors: Tsuneo Yamaguchi, Akira Saito, Akio Kato
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Publication number: 20140080736Abstract: Tumour marker proteins and their preparation from fluids from one or more cancer patients, wherein said fluids are those which collect in a body cavity or space which is naturally occurring or which is the result of cancer or medical intervention for cancer. The present application also relates to preparation of tumour marker proteins from excretions taken from patients with cancer. The tumour marker proteins are useful as immunoassay reagents in the detection of cancer-associated anti-tumour marker autoantibodies.Type: ApplicationFiled: November 19, 2013Publication date: March 20, 2014Applicant: Onclmmune LimitedInventors: John Forsyth Russell Robertson, Catherine Rosamund Louise Graves
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Patent number: 8674073Abstract: Provided is affinity chromatography carrier for an immunoglobulin that simultaneously has high immunoglobulin-binding capability and chemical stability and that can be produced at low cost. An immunoglobulin-binding protein in which an amino acid substitution for not only maximizing the number of lysine residues on the protein surface of helix 3 and its periphery but also minimizing the number of lysine residues present on the protein surfaces of helix 1 and helix 2 as immunoglobulin-binding regions and/or an amino acid substitution for eliminating an aspartic acid-proline sequence have (has) been carried out, or a multimer thereof, is used as an affinity ligand for an affinity chromatography carrier.Type: GrantFiled: February 21, 2007Date of Patent: March 18, 2014Assignee: Protenova Co., Ltd.Inventors: Eiji Majima, Atsushi Shima, Yuko Hara
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Patent number: 8673385Abstract: A soy protein product having a protein content of at least about 60 wt % (N×6.25) d.b., preferably an isolate having a protein content of at least about 90 wt % (N×6.25) d.b., is formed by extracting a soy protein source with water to form an aqueous protein solution having a pH of about 1.5 to about 11, preferably about 5 to about 7, and separating the resulting aqueous protein solution from residual soy protein source. The protein concentration of the aqueous protein solution is increased to about 50 to about 400 g/L while the ionic strength is maintained substantially constant by using a selective membrane technique. The resulting concentrated protein solution is optionally diafiltered and a calcium salt, preferably calcium chloride, is added to the concentrated and optionally diafiltered protein solution to a conductivity of 5 to about 30 mS.Type: GrantFiled: June 30, 2010Date of Patent: March 18, 2014Assignee: Burcon Nutrascience (MB) Corp.Inventors: Kevin I. Segall, Martin Schweizer, Brent E. Green, Sarah Medina, Brandy Gosnell
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Patent number: 8669075Abstract: The present invention relates to a method for immobilization of a biologically active polypeptide using maltose binding protein (MBP) and a biologically active solid substrate on which a biologically active polypeptide is immobilized by the above method. More particularly, the present invention relates to a method for immobilization of a biologically active polypeptide comprising the following steps; 1) preparing a fusion protein by linking a biologically active polypeptide to carboxyl terminal of maltose binding protein (MBP); and 2) immobilizing the fusion protein on the hydrophobic surface by physical adsorption of amino terminal containing hydrophobic domain exposed on the surface of maltose binding protein on the hydrophobic surface of a solid substrate, and a biologically active solid substrate on which a biologically active polypeptide is immobilized by the said method.Type: GrantFiled: October 24, 2008Date of Patent: March 11, 2014Assignee: Korea Institute of Science and TechnologyInventors: Sang-Heon Kim, Soo Hyun Kim, Min Han
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Patent number: 8669348Abstract: The present invention relates to a novel hypoglycemic/anti-hyperglycemic protein named ADMc1 purified from the seeds of Momordica charantia for control of hyperglycemia. The process for the purification of novel hypoglycemic/anti-hyperglycemic protein named ADMc1 is also disclosed. The invention also relates to process for preparation and purification of the recombinant novel hypoglycemic/anti-hyperglycemic protein of Momordica charantia, named rADMc1. Both ADMc1 and rADMc1 are highly effective and need to be administered only once a day to maintain normal blood glucose levels. The procedure involves purification of a novel hypoglycemic/anti-hyperglycemic protein of M. charantia, construction of cDNA library from M. charantia seeds, screening of cDNA library using oligonucleotide probe designed on the basis of amino acid sequence of the tryptic fragment of the protein, cloning of the cDNA in a eukaryotic expression system, expression and purification of the recombinant protein.Type: GrantFiled: March 28, 2008Date of Patent: March 11, 2014Inventors: Aparna Dixit, Aruna Vashishta, Tejram Sahu, Shailesh Kumar Choudhary, Alli Murugesan
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Patent number: 8669353Abstract: The present invention concerns a process for producing compositions that are rich in secretory IgA (S-IgA) by fractionating milk containing S-IgA. Such compositions may be used in particular for treating and/or preventing infections and/or inflammation of the mucosal surfaces, e.g. the gastro-intestinal tract, urogenital tract, respiratory tract, nasal cavity or oral cavity, treating and/or preventing obesity and related diseases, or treating and/or preventing food allergies in subjects in need of such treatment. Briefly stated, the current invention provides a process for producing milk fractions rich in secretory Immunoglobulin A, using one or more microporous membrane filtration steps. A preferred protocol of the present process involves de-fatting, micro-filtration and ultrafiltration-concentration through a number of diafiltration cycles.Type: GrantFiled: May 11, 2009Date of Patent: March 11, 2014Assignee: W. Health L.P.Inventors: Charles Maria Hubert Hensgens, Nanda De Groot
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Patent number: 8663990Abstract: A subject of the present invention is to provide a measurement method using an internal standard substance in an electrophoresis where an analyte is a protein or a compound. The present invention relates to a measurement method for an analyte by an electrophoresis, characterized in that a peak of the analyte is identified by using as an internal standard substance (1) a combination of a compound I having 3 or more anion groups in a molecule and a compound II where 1 to 3 groups of the anion groups of said compound I have been substituted by cation groups, or (2) a combination of a compound III having 3 or more cation groups in a molecule and a compound IV where 1 to 3 groups of the cation groups of said compound III have been substituted by cation groups.Type: GrantFiled: April 27, 2010Date of Patent: March 4, 2014Assignee: Wako Pure Chemical Industries, Ltd.Inventors: Naoyuki Yamamoto, Tatsuo Kurosawa
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Patent number: 8663950Abstract: The present invention describes the plant-based production of a therapeutic antibody against West Nile Virus.Type: GrantFiled: January 10, 2011Date of Patent: March 4, 2014Assignee: Arizona Board of RegentsInventors: Qiang Chen, Huafang Lai
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Patent number: 8658773Abstract: Disclosed are methods, compositions and uses of high concentration antibody or immunoglobulin formulations for subcutaneous, intramuscular, transdermal or other local (regional) administration, in a volume of than 3, less than 2 or less than 1 ml. Preferably, the formulation contains a high concentration formulation (HCF) buffer comprising phosphate, citrate, polysorbate 80 and mannitol at a pH of about 5.2. The formulation more preferably comprises at least 100, 150, 200, 250 mg/ml or 300 mg/ml of antibody. The methods for preparing the high concentration formulation include ultrafiltration and diafiltration to concentrate the antibody and exchange the medium for HCF buffer. Other embodiments concern use of non-G1m1 (nG1m1) allotype antibodies, such as G1m3 and/or a nG1m1,2 antibodies. The nG1m1 antibodies show decreased immunogenicity compared to G1m1 antibodies.Type: GrantFiled: May 1, 2012Date of Patent: February 25, 2014Assignee: Immunomedics, Inc.Inventors: Li Zeng, Rohini Mitra, Edmund A. Rossi, Hans J. Hansen, David M. Goldenberg
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Patent number: 8658772Abstract: Methods for selective extraction and fractionation of algal proteins from an algal biomass or algal culture are disclosed. A method of selective removal of products from an algal biomass provides for single and multistep extraction processes which allow for efficient separation of algal proteins. These proteins can be used as renewable sources of proteins for animal feedstocks and human food. Further, lipids remaining in the algal biomass after extraction of proteins can be used to generate renewable fuels.Type: GrantFiled: October 13, 2011Date of Patent: February 25, 2014Assignee: Heliae Development, LLCInventor: Aniket Kale
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Patent number: 8653245Abstract: This invention relates to protein separation and purification methods for both alpha-1-antitrypsin (AAT, also known as alpha-1 proteinase inhibitor, API, and A.sub.1-PI) and Apolipoprotein A-I (ApoA-1) from, for example, a fraction of human blood plasma. In certain embodiments, the invention provides methods for separating AAT from ApoA-1 at the initial stage of purification, so that the same starting material can be used as a source for both proteins. The methods further pertain to providing compositions of AAT and of ApoA-1 suitable for pharmaceutical use and are suitable for large-scale purification.Type: GrantFiled: April 5, 2013Date of Patent: February 18, 2014Assignee: CSL Behring GmbHInventors: Nathan Brinkman, Douglas Bigler, Reinhard Bolli, Vreni Foertsch
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Patent number: 8653246Abstract: The present invention provides a method for purifying a protein to remove impurities from a mixture liquid containing a desired protein and the impurities, comprising the step of performing filtration using a porous membrane having a graft chain on a pore surface and an anion-exchange group fixed to the graft chain.Type: GrantFiled: September 26, 2008Date of Patent: February 18, 2014Assignee: Asahi Kasei Chemicals CorporationInventors: Hironobu Shirataki, Naoyuki Shinohara
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Patent number: 8652849Abstract: This invention relates to a composite material that comprises a support member that has a plurality of pores extending through the support member and, located in the pores of the support member, and filling the pores of the support member, a macroporous cross-linked gel. The invention also relates to a process for preparing the composite material described above, and to its use. The composite material is suitable, for example, for separation of substances, for example by filtration or adsorption, including chromatography, for use as a support in synthesis or for use as a support for cell growth.Type: GrantFiled: October 14, 2008Date of Patent: February 18, 2014Assignee: Natrix Separations Inc.Inventors: Ronald F. Childs, Carlos Filipe, Raja Ghosh, Alicja M. Mika, Jinsheng Zhou, Elena N. Komkova, Marcus Y. Kim, Tapan K. Dey
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Patent number: 8653032Abstract: Disclosed is a pharmaceutical composition for preventing or treating TRPV1 activity-related or inflammation-related, diseases or conditions, containing a Maillard peptide separated from well-aged traditional soy sauce as an active ingredient. The Maillard peptide in the present invention functions both as a TRPV1 agonist and a TRPV1 antagonist, and further functions as a TRPV1 activity modulator. Therefore, the Maillard peptide can be used for preventing or treating TRPV1 activity-related diseases such as pain, neurological diseases, urgent defecation, inflammatory bowel disease, respiratory diseases, urinary incontinence, overactive bladder, neurogenic / allergic / inflammatory skin diseases, skin, eye or mucosal irritation, hyperacusis, tinnitus, vestibular hypersensitivity, heart disease, etc.Type: GrantFiled: November 8, 2010Date of Patent: February 18, 2014Assignees: Korea Food Research Institute, SNU R & DB FoundationInventors: Mee-Ra Rhyu, Ah-Young Song, Eun-Young Kim, Seog Bae Oh, YoungJoo Lee, Won Chung Lim
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Patent number: 8648178Abstract: The present invention relates to a method for purifying a protein belonging to the TGF-?, superfamily, preferably BMP, and more preferably BMP-2. According to the invention, the number of purification steps is reduced and the purification process is simplified, compared to the conventional BMP-2 purification method. Thus, the time required for purification can be shortened and the cost can be reduced. In addition, the invention solves the problem that as the time for purification increases and the number of purification steps increases, BMP-2 is degraded by protease or lost during purification steps, resulting in a decrease in the final yield of BMP-2. Thus, the invention increases the final yield of BMP-2.Type: GrantFiled: May 12, 2010Date of Patent: February 11, 2014Assignee: Korea Bone Bank Co., Ltd.Inventors: Young-Bock Shim, Yeong-Schick Kim, Yon-Rak Choi, Ju-Woong Jang
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Patent number: 8642276Abstract: The present invention relates to a method for producing or identifying a MUC1 molecule which is able to generate an immune response in humans. The invention also relates to a method for producing or identifying a cell, cell lines or cell lysates containing a MUC1 molecule that is able to generate an immune response in humans. The invention further relates to methods for producing medicaments and diagnostic agents. Also disclosed is the use of the MUC1 molecules, cells or cell lysates obtained by means of the methods according to the invention for producing a medicament used for treating or preventing tumors. Further disclosed is a purified MUC1 molecule that can be obtained by means of the methods according to the invention and has an immunostimulating effect on humans. The invention additionally relates to the use of a MUC1 antibody for the production of a medicament used for treating or preventing tumors.Type: GrantFiled: June 18, 2010Date of Patent: February 4, 2014Assignee: Glycotope GmbHInventors: Steffen Goletz, Uwe Karsten
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Patent number: 8642745Abstract: The invention relates to a method of preparing heteromultimeric polypeptides such as bispecific antibodies, bispecific immunoadhesins and antibody-immunoadhesin chimeras. The invention also relates to the heteromultimers prepared using the method. Generally, the method provides a multispecific antibody having a common light chain associated with each heteromeric polypeptide having an antibody binding domain. Additionally the method further involves introducing into the multispecific antibody a specific and complementary interaction at the interface of a first polypeptide and the interface of a second polypeptide, so as to promote heteromultimer formation and hinder homomultimer formation; and/or a free thiol-containing residue at the interface of a first polypeptide and a corresponding free thiol-containing residue in the interface of a second polypeptide, such that a non-naturally occurring disulfide bond is formed between the first and second polypeptide.Type: GrantFiled: December 8, 2006Date of Patent: February 4, 2014Assignee: Genentech, Inc.Inventors: W. Robert Arathoon, Paul J. Carter, Anne M. Merchant, Leonard G. Presta
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Publication number: 20140031531Abstract: A method for producing a target protein is provided, which includes steps described below. A crude extract including a fusion protein is provided. The fusion protein includes a tag, a target protein and a linker inserted between the tag and the target protein. The fusion protein and magnetic particles are then bound to form a magnetic particle-binding fusion protein. Finally, the linker of the magnetic particle-binding fusion protein undergoes autocleavage by using a cleavage buffer solution to release the target protein. A one-pot process for producing a purified target protein is also provided.Type: ApplicationFiled: January 29, 2013Publication date: January 30, 2014Applicant: NATIONAL CHIAO TUNG UNIVERSITYInventors: Yaw-Kuen LI, Yue-Jin WU
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Patent number: 8637037Abstract: The present invention concerns the preparation of purified allergens and allergoids, both derived from whole bee venom, for the desensitization (immunotherapy) of subjects affected by a specific allergy. In particular, the present invention concerns a preparation for immunotherapy based on purified bee venom, characterized in that said bee venom is essentially mellitin-free. In addition, the preparation of a monomeric allergoid obtainable through the carbamylation or thiocarbamylation reaction of said mellitin-free bee venom, is described. Said allergoid, being characterized by reduced IgE-binding activity, may be a safer and more effective candidate for specific immunotherapy.Type: GrantFiled: December 16, 2008Date of Patent: January 28, 2014Assignee: Lofarma S.p.A.Inventors: Giovanni Mistrello, Daniela Roncarolo, Dario Zanoni, Paolo Falagiani