Chromatography Or By Septum Selective As To Material, E.g., Gel Filtration, Molecular Sieve Dialysis, Etc. Patents (Class 530/417)
  • Publication number: 20120016113
    Abstract: A buoyant device containing chromatography media performs the function of protein harvesting replacing the steps of cell separation and volume reduction; the device can be loaded into columns for further purification.
    Type: Application
    Filed: September 26, 2011
    Publication date: January 19, 2012
    Applicant: Therapeutic Proteins Inc
    Inventor: Sarfaraz K. Niazi
  • Publication number: 20120010390
    Abstract: The present invention relates to a process of enriching one target compound from a liquid, which process comprises at least one step of isolation performed by differentially partitioning between two aqueous phases. In the present invention the phases are formed by adding a thermally responsive, self-associating (i.e. clouding) hydrophilic polymer, and if needed some additional salts, to an aqueous biotechnical solution (such as a fermentation sample or bioseparation process stream) under thermal and other conditions where the solution separates into a one polymer, two-phase system with one phase enriched in the polymer. The target compound is to be found in the phase not enriched in the polymer, while a significant though varying percentage of contaminants may differentially partition to the phase interface or the polymer enriched phase.
    Type: Application
    Filed: January 7, 2010
    Publication date: January 12, 2012
    Inventors: James Van Alstine, Jamil Shanagar, Rolf Hjorth, Martin Hall, Camilla Estmer Nilsson
  • Patent number: 8084224
    Abstract: A method to facilitate recovery troponin I and/or troponin T from a sample comprising addition of troponin C to the sample or to a surface from which the troponin I and/or troponin T are recovered.
    Type: Grant
    Filed: April 5, 2010
    Date of Patent: December 27, 2011
    Assignee: Alere San Diego, Inc.
    Inventors: Kenneth F. Buechler, Paul H. McPherson
  • Patent number: 8080272
    Abstract: The present invention relates to methods for the separation of various components from eggs. More particularly, the present invention relates to methods for the separation of proteins and lipids from eggs, including technical eggs (inedible) or edible eggs, yolks or whites, which comprises cross-linking the lipids of eggs with a cross-linking reagent. In an embodiment, the method includes separating the proteins from the cross-linked lipids. In an embodiment, the method includes the separation of various components associated with the cross-linked lipids. The methods disclosed herein allow for the isolation of multiple different components from the egg in an efficient, cost-effective manner without compromising the recovery process of the components or their subsequent utility in various applications or compositions. The compositions and isolated components obtained by the methods of the invention can be used in pharmaceutical, medical, nutritional, cosmetic or health applications.
    Type: Grant
    Filed: January 9, 2008
    Date of Patent: December 20, 2011
    Assignee: Biova, L.L.C.
    Inventors: Ronald E. Strohbehn, Jesse I. Figgins
  • Publication number: 20110301333
    Abstract: The present invention provides novel and improved compositions containing calcium phosphate and methods of using the same for the removal of protein aggregates from biopharmaceutical compositions containing a product of interest, e.g., a therapeutic antibody or protein.
    Type: Application
    Filed: May 10, 2011
    Publication date: December 8, 2011
    Applicant: Millipore Corporation
    Inventors: Ajish Potty, Alex Xenopolous
  • Publication number: 20110301342
    Abstract: The invention is directed to an apparatus and method for purifying a protein. The apparatus involves the use of a capture chromatography resin, a depth filter arranged after the capture chromatography resin, and a mixed-mode chromatography resin arranged after the depth filter. The method involves providing a sample containing the protein, processing the sample through a capture chromatography resin, a depth filter, and a mixed-mode chromatography resin. A membrane adsorber or monolith may be substituted for the mixed-mode chromatography column.
    Type: Application
    Filed: April 13, 2011
    Publication date: December 8, 2011
    Inventors: Chen Wang, Robert K. Hickman, Edwin O. Lundell, Roy D. Hegedus
  • Patent number: 8058411
    Abstract: The present invention relates to a method for producing a mature von Willebrand Factor (VWF) from von Willebrand Factor pro-peptide comprising the steps: immobilizing VWF pro-peptide on an ion exchange resin, incubating the immobilized VWF pro-peptide with furin to obtain immobilized mature VWF, and isolating mature VWF from the ion exchange resin by elution.
    Type: Grant
    Filed: May 16, 2008
    Date of Patent: November 15, 2011
    Assignees: Baxter International Inc., Baxter Healthcare S.A.
    Inventors: Wolfgang Mundt, Artur Mitterer, Meinhard Hasslacher, Christa Mayer
  • Patent number: 8058014
    Abstract: The present invention is directed to methods of diagnosing a disease or predicting an increased risk of a disease, such as obesity, obesity-dependent subacute inflammation, atherosclerosis, cardiovascular disease and a metabolic disease, by determining the levels of omentin 1 and 2 protein in a subject, or by determining the levels of omentin 1 and 2 gene expression in a subject. The present invention is also directed to methods of disease treatment using omentin 1 protein and omentin 2 protein.
    Type: Grant
    Filed: September 29, 2007
    Date of Patent: November 15, 2011
    Assignee: University of Maryland, Baltimore
    Inventors: Da-Wei Gong, John C. McLenithan, Alan R. Shuldiner, Rong-Ze Yang
  • Publication number: 20110263834
    Abstract: This invention is directed to methods for removing, preferably simultaneously and in one step, multiple impurities form crude culture samples, and, in particular, the removal of media components, protein, nucleic acids, lipids, and lipopolysaccharides to ultralow levels. Preferably the purification process comprises: (1) binding of the target substance containing one or more contaminants to a chromatography matrix; (2) washing the bound target substance with one or more buffers containing a synergistic combination of a lyotropic agent or organic solvent, a detergent, and a salt component; and (3) desorbing the target substance from the chromatography matrix, so that the eluate contains ultra low levels of contaminants. The reduction of impurities that can be achieved is preferably 91-99.9% as compared to the amount of impurities in the target substance before purification. The invention is also directed to the targets products that have been so purified.
    Type: Application
    Filed: December 20, 2010
    Publication date: October 27, 2011
    Applicants: FinaBioSolutions, LLC, Serum Institute of India, Ltd.
    Inventors: Andrew Lees, Jayant Sakaram Joshi
  • Patent number: 7998705
    Abstract: The present invention generally relates to novel processes for protein purification in high salt solutions such as cell culture broth by increasing the dynamic binding capacity of a resin with the addition of polyethylene glycol.
    Type: Grant
    Filed: November 12, 2002
    Date of Patent: August 16, 2011
    Assignee: FUJIFILM Diosynth Biotechnologies U.S.A., Inc
    Inventors: Min Wan, Mark David Chavez, Jeffrey Lee Schrimsher
  • Publication number: 20110150911
    Abstract: Immunogenic compositions for use in treating, preventing and diagnosing infection caused by the California (CAL) serotype of the genus Bunyavirus, such as La Crosse virus (LACV), are disclosed. Also described are reagents for use in diagnostic assays.
    Type: Application
    Filed: November 19, 2004
    Publication date: June 23, 2011
    Inventors: Qui-Lim Choo, Michael Houghton, Elizabeth Scott, Amy Weiner
  • Patent number: 7959926
    Abstract: The present invention relates generally to the production, purification, and isolation of human growth hormone (hGH). More particularly, the invention relates to the production, purification, and isolation of substantially purified hGH comprising non-naturally encoded amino acids and hGH from recombinant host cells or culture medium including, for example, yeast, insect, mammalian and bacterial host cells. The process of the present invention is also useful for purification of hGH linked to polymers or other molecules.
    Type: Grant
    Filed: October 17, 2007
    Date of Patent: June 14, 2011
    Assignee: Ambrx, Inc.
    Inventors: Ying Buechler, Ricky Lieu, Michael Ong, Stuart Bussell, Nick Knudsen, Ho Sung Cho
  • Publication number: 20110120947
    Abstract: There is provided a crosslinked cellulose hydrate membrane having a porous double structure which consists of micropores having a diameter in the range from >100 nm to 20 ?m and ultrapores which have a diameter of <100 nm and which are not accessible to Blue Dextran having an average molecular weight Mw of 2 000 000, wherein the fraction of the volume of the ultrapores is more than 15% of the entire pore volume accessible to water, and wherein hydrophobic ligands, selected from C1-C20-alkyl and their derivatives or C6-C25-aryl and their derivatives or C7-C25-arylalkyl and their derivatives or —[(CH2)m—O—]n—R, where m is 2 or 3, n is a whole number greater than or equal to 1, and R is —H or —C1-C5-alkyl, are bonded to the membrane. In addition, methods for producing the membrane, an apparatus for hydrophobic interaction chromatography and comprising the membrane, and the use of the membrane in hydrophobic interaction chromatography are specified.
    Type: Application
    Filed: February 10, 2009
    Publication date: May 26, 2011
    Inventor: René Faber
  • Patent number: 7943046
    Abstract: Embodiments of the present invention provide a method of chromatographic delipidation comprising separating a lipid-containing sample on a superficially porous stationary phase at greater than about 70° C., at least about 80° C., having at least one mobile phase comprising an ion-pairing agent in water, an ion-pairing agent in an organic modifier, an acid in an organic modifier, and an alcohol. The invention provides minimal protein losses and high run-to-run reproducibility. The on-column delipidation method aventageously utilize reversed phase liquid chromatography.
    Type: Grant
    Filed: June 22, 2006
    Date of Patent: May 17, 2011
    Assignee: Agilent Technologies, Inc
    Inventors: James D. Martosella, Nina I. Zolotarjova
  • Patent number: 7928191
    Abstract: A method for purifying bioactive substances includes the steps of: causing a bioactive substance having histidine units to contact media, each constituted by a substrate, ligands which are physically attached to the surface of the substrate, and Cu(II) or Fe(II) metal ions which are covalently bonded to the ligands; causing the bioactive substance to covalently bond with the metal ions via the histidine units; and washing the media with an amount of 1 nmol/L to 10 mmol/L imidazole derivative solution 60 times the volume of the media or greater. In the case that the metal ions are Cu(II), the bioactive substance which has covalently bonded with the Cu(II) via the histidine units are recovered by one of a 10 mmol/L to 1 mol/L imidazole derivative solution and a 0.5 mmol/L to 5 mol/L EDTA solution.
    Type: Grant
    Filed: August 29, 2008
    Date of Patent: April 19, 2011
    Assignee: Fujifilm Corporation
    Inventors: Koichi Minami, Yohsuke Takeuchi, Taisei Nishimi
  • Publication number: 20110082283
    Abstract: ELP fusion proteins, multimeric ELP spider complexes formed of ELP fusion proteins, and methods of using the same. The construct may be in the form of an ELP spider structure complex including multi-leg moieties comprising ELP fusion proteins capable of forming covalent disulfide bonds. The multimeric fusion constructs may be employed in peptide production and purification and/or to enhance proteolytic resistance of a protein or peptide moiety in a fusion construct, by provision of the fusion protein in an ELP spider complex.
    Type: Application
    Filed: February 25, 2010
    Publication date: April 7, 2011
    Inventor: Suzanne DAGHER
  • Publication number: 20110065897
    Abstract: The present invention relates to a method for isolating and/or purifying at least one polypeptide from a polypeptide-containing sample, characterized in that the sample is contacted with a boron carbide support material at a pH which allows the binding of the polypeptide to the boron carbide support material. Such isolating can, for example, be used to remove polypeptides from a sample or else to purify and/or to concentrate polypeptides. A matrix comprising a boron carbide support material for purification of polypeptides is further disclosed according to the invention.
    Type: Application
    Filed: April 9, 2009
    Publication date: March 17, 2011
    Inventor: Christian Feckler
  • Patent number: 7901911
    Abstract: The present invention intends to provide an IL-6R.IL-6 fusion protein and the like in which IL-6R and IL-6 are directly linked without a linker. The IL-6 receptor.IL-6 fusion protein of the present invention has a structure in which one amino acid residue constituting IL-6 receptor and one amino acid residue constituting IL-6 are directly bonded.
    Type: Grant
    Filed: March 19, 2009
    Date of Patent: March 8, 2011
    Assignee: Tosoh Corporation
    Inventors: Teiji Ekida, Harutaka Yagame, Hiroshi Iida, Kiyoshi Yasukawa, Shigeo Tsuchiya, Teruhiko Ide
  • Patent number: 7858341
    Abstract: The expression vectors and methods using an E. coli expression system for the large scale production of FGF18 are described. The vectors utilize the FGF18 coding sequence with specific changes in nucleotides in order to optimize codons and mRNA secondary structure for translation in E. coli. Using the expression vectors, the FGF18 gene was produced in E. coli to a level of greater than 1 g/L in fed batch fermentation. Also included are OmpT deficient E. coli strains, as well as OmpT and fhuA negative strains transformed with an FGF18 expression vector.
    Type: Grant
    Filed: December 12, 2005
    Date of Patent: December 28, 2010
    Assignee: ZymoGenetics, Inc.
    Inventors: Brian J. Reardon, Susan H. Julien, Chung-leung Chan, Hong Y. Liu
  • Publication number: 20100311953
    Abstract: The invention relates to a process for purifying a protein by mixing a protein preparation with a solution having a first salt and a second salt, wherein each salt has a different lyotropic value, and loading the mixture onto a hydrophobic interaction chromatography column. The dynamic capacity of the column for a protein using the two salt combination will be increased compared with the dynamic capacity of the column for either single salt alone.
    Type: Application
    Filed: June 23, 2010
    Publication date: December 9, 2010
    Applicant: Amgen Inc.
    Inventors: Anna Senczuk, Ralph Klinke
  • Publication number: 20100310539
    Abstract: The present invention relates to a new synthetise for the preparation of mesoporous structures including mesoporous materials with chiral morphologies and mesoporous materials with local or surface chirality. The method can be used for manufacturing controlled drug delivery devices, for example for delivery of folic acid, and fluorescent particles.
    Type: Application
    Filed: February 11, 2009
    Publication date: December 9, 2010
    Inventor: Alfronso Garcia-Bennett
  • Publication number: 20100286071
    Abstract: Members of the TGF-? superfamily and peptide fragments based on member proteins are employed to purify solutions containing member proteins or as therapeutics.
    Type: Application
    Filed: June 17, 2010
    Publication date: November 11, 2010
    Applicant: Wyeth LLC
    Inventors: Zhijian Lu, Wei Liu, Jimin Zhang, Paul John Yaworsky, Stephane H. Olland, Christopher Todd Brown, Emily Sheng-ming Shen
  • Patent number: 7820800
    Abstract: The invention relates to a process for the purification of IL-18 binding protein (IL-18BP) from a fluid comprising hydrophobic charge-induction chromatography.
    Type: Grant
    Filed: November 4, 2004
    Date of Patent: October 26, 2010
    Assignee: Ares Trading S.A.
    Inventors: Mara Rossi, Thierry Ziegler, Laure Valognes
  • Patent number: 7816495
    Abstract: The present invention relates to processes for the purification of fibrinogen, and to readily solubilised fibrinogen preparations.
    Type: Grant
    Filed: July 7, 2003
    Date of Patent: October 19, 2010
    Assignee: NHS Blood and Transplant
    Inventors: Sarah Kingsland, Robert Clemmitt, David Evans, Peter Feldman
  • Publication number: 20100261886
    Abstract: The invention provides methods for isolating proteins in purified form from mixtures by precipitation with citrate. The methods are advantageous in that they effectively separate a protein from lower molecular weight contaminants, including fragments or portions of the protein. Such methods are particularly useful for purifying antibodies from mixtures containing antibody proteolytic fragments and unpaired chains.
    Type: Application
    Filed: April 13, 2010
    Publication date: October 14, 2010
    Applicant: Bristol-Myers Squibb Company
    Inventors: Alahari Arunakumari, Gisela M. Ferreira
  • Patent number: 7795405
    Abstract: After the sequencing of the human genome, great interest has developed in trying to discern the complementary proteome of humans and other species. The present disclosure provides devices, systems, and methods for proteomic fractionation that may increase the number of protein spots visualized by 2DE analysis, and may allow enrichment of proteins normally not detectable by standard 2DE analysis. According to some embodiments of the disclosure, devices, systems, and methods of the disclosure relate to fractionating a proteome on the basis of surface charge, hydrophobicity, isoelectric point and/or size.
    Type: Grant
    Filed: January 29, 2007
    Date of Patent: September 14, 2010
    Assignee: Guild Associates, Inc.
    Inventor: Augustine DiNovo
  • Patent number: 7771725
    Abstract: The invention concerns a new medicinal product for the treatment of arboviruses, i.e.. a concentrate of immunoglobulins and F(ab)?2 and/or Fab fragments specific to said arbovirus as well as its process of preparation.
    Type: Grant
    Filed: April 2, 2007
    Date of Patent: August 10, 2010
    Assignee: Laboratoire Fancais du Fractionnement et des Biotechnologies
    Inventor: Roland Schmitthaeusler
  • Patent number: 7756646
    Abstract: A method of predicting whether a peptide present in a biological sample will be detected by analysis with a mass spectrometer. The method uses at least one mass spectrometer to perform repeated analysis of a sample containing peptides from proteins with known amino acids. The method then generates a data set of peptides identified as contained within the sample by the repeated analysis. The method then calculates the probability that a specific peptide in the data set was detected in the repeated analysis. The method then creates a plurality of vectors, where each vector has a plurality of dimensions, and each dimension represents a property of one or more of the amino acids present in each peptide and adjacent peptides in the data set. Using these vectors, the method then generates an algorithm from the plurality of vectors and the calculated probabilities that specific peptides in the data set were detected in the repeated analysis.
    Type: Grant
    Filed: March 31, 2006
    Date of Patent: July 13, 2010
    Assignee: Battelle Memorial Institute
    Inventors: Lars Kangas, Richard D. Smith, Konstantinos Petritis
  • Patent number: 7754860
    Abstract: The invention provides a method for purifying recombinant FSH.
    Type: Grant
    Filed: December 16, 2004
    Date of Patent: July 13, 2010
    Assignee: Ares Trading S.A.
    Inventor: Mara Rossi
  • Patent number: 7754689
    Abstract: Members of the TGF-? superfamily and peptide fragments based on member proteins are employed to purify solutions containing member proteins or as therapeutics.
    Type: Grant
    Filed: June 1, 2007
    Date of Patent: July 13, 2010
    Assignee: Wyeth LLC
    Inventors: Zhijian Lu, Wei Liu, Jimin Zhang, Paul John Yaworsky, Stephane H. Olland, Christopher Todd Brown, Emily Sheng-ming Shen
  • Patent number: 7745582
    Abstract: The present invention relates to a novel method for the isolation or purification of immunoglobulins (a special class of proteins) from a solution containing immunoglobulins, e.g. hybridoma cell culture supernatants, animal plasma or sera, or colostrum. The method includes the use of a minimum of salts, such as lyotropic salts, in the binding process and preferably also the use of small amounts of organic solvents in the elution process. The solid phase matrices, preferably epichlorohydrin activated agarose matrices, are functionalised with mono- or bicyclic aromatic or heteroaromatic ligands (molecular weight: at the most 500 Dalton) which, preferably, comprises an acidic substituent, e.g. a carboxylic acid. The matrices utilised show excellent properties in a “Standard Immunoglobulin Binding Test” and in a “Monoclonal Antibody Array Binding Test” with respect to binding efficiency and purity, and are stable in 1M NaOH.
    Type: Grant
    Filed: October 31, 2007
    Date of Patent: June 29, 2010
    Assignee: Upfront Chromatography
    Inventors: Allan Otto Fog Lihme, Marie Bendix Hansen
  • Patent number: 7744890
    Abstract: Methods for reducing the opalescent appearance of a protein preparation by modifying the ionic strength of the preparation, as well as compositions, e.g., pharmaceutical compositions, of concentrated protein with decreased opalescence are disclosed. Purification methods which monitor and/or reduce the salt concentrations at selected steps are also disclosed.
    Type: Grant
    Filed: October 12, 2007
    Date of Patent: June 29, 2010
    Assignee: Wyeth LLC
    Inventors: Pilarin Elizabeth Nichols, Donna L. Luisi
  • Publication number: 20100160605
    Abstract: To provide a novel packing material for liquid chromatography capable of separating and purifying, or collecting and recovering, a biopolymer such as a protein or a peptide by adsorption and desorption by a pH change without being influenced by the isoelectric point of the protein or by the salt concentration in a solvent in which the biopolymer such as the protein is dissolved, and to provide a process for concentrating and recovering a desired biopolymer such as a protein or a peptide from a large amount of dilute cell culture solution by means of such a packing material.
    Type: Application
    Filed: December 17, 2009
    Publication date: June 24, 2010
    Inventors: Katsuo KOMIYA, Koji NAKAMURA
  • Publication number: 20100151581
    Abstract: The present invention relates to a separation matrix comprised of a porous support to which ligands have been immobilised, wherein said ligands comprise at least one aliphatic sulphonamide. The nitrogen of the sulphonamide may be a secondary or tertiary amine. The invention also relates to a chromatography column that contains the described separation matrix, as well as to a method of isolating immunoglobulin-like compounds by adsorption to a separation matrix that comprises aliphatic sulphonamide ligands.
    Type: Application
    Filed: February 22, 2010
    Publication date: June 17, 2010
  • Publication number: 20100144622
    Abstract: Methods of producing properly refolded recombinant plasminogen and plasmin polypeptide are provided. Denatured recombinant plasminogen polypeptide is refolded by first solubilizing the polypeptide with a chaotroph and reducing and oxidizing agents at high pH, followed by refolding in the presence of reduced concentration of chaotroph and reducing and oxidizing agents and in the presence of arginine.
    Type: Application
    Filed: September 28, 2007
    Publication date: June 10, 2010
    Inventors: Xinli Lin, Daniel Medynski
  • Patent number: 7728116
    Abstract: In a method of isolating osteogenic protein from bone, in which an osteogenic protein-containing fraction is extracted from bone and enriched by a sequence of enrichment steps selected from ultrafiltration and chromatography, the invention provides the improvement of removing higher molecular weight components from the osteogenic protein-containing fraction prior to the enrichment steps. The higher molecular weight components have a molecular weight of about 100-300 kDa and are selected from collagen, collagen fragments, collagen aggregates and mixtures thereof.
    Type: Grant
    Filed: June 18, 2003
    Date of Patent: June 1, 2010
    Assignee: Altis Biologics (Proprietary) Limited
    Inventor: Nicolaas Duneas
  • Patent number: 7723492
    Abstract: Uses of recombinant procalcitonin 3-116 in the diagnosis and therapy of septic diseases and the measurement of prohormones other than procalcitonin, and of dipeptidyl peptidase IV, as biomarkers in the diagnosis of sepsis.
    Type: Grant
    Filed: September 29, 2008
    Date of Patent: May 25, 2010
    Assignee: B.R.A.H.M.S. Aktiengesellschaft
    Inventors: Andreas Bergmann, Joachim Struck, Wolfgang Weglöhner
  • Patent number: 7718845
    Abstract: The invention relates to a method of producing a protein of interest, comprising making a non-human transgenic mammal that produces said protein in its milk, obtaining said milk from the non-human transgenic mammal and purifying said protein of interest from the milk. Transgenic bovine animals were generated, which are able to produce human growth hormone in mammary glands. The method involves cloning of a genetic construct encoding hGH gene and beta casein promoter conveniently in an expression vector. It also includes transfection procedures into fetal bovine somatic cells, generally fibroblasts, and the nuclear transfer into enucleated bovine oocytes, generating thus transgenic embryos.
    Type: Grant
    Filed: September 29, 2004
    Date of Patent: May 18, 2010
    Assignee: Sterrenbeld Biotechnologie North America, Inc.
    Inventors: Carlos Alberto Melo, Lino Baranao, Cesar Horacio Carbonetto
  • Publication number: 20100113751
    Abstract: The present invention provides a method of removing product-related inactive or partially active species, high molecular weight aggregates, as well as other process-related impurities from preparations of acidic proteins by using ceramic hydroxyapatite chromatography.
    Type: Application
    Filed: October 29, 2009
    Publication date: May 6, 2010
    Applicant: Wyeth
    Inventors: Shujun Sun, Yin Luo, Priscilla Jennings
  • Publication number: 20100105871
    Abstract: The invention relates to a process for the removal of glycoalkaloids, in particular from process streams such as those encountered during isolation of proteins from potatoes.
    Type: Application
    Filed: October 25, 2007
    Publication date: April 29, 2010
    Inventors: Marco Luigi Federico Giuseppin, Robin Eric Jacobus Spelbrink
  • Patent number: 7695973
    Abstract: The present invention provides methods for quantitation of glycated protein in a biological sample using a solid support matrix by making a first bound protein measurement total bound protein under conditions where both glycated and non-glycated protein bind to the support in making a second bound protein measurement under conditions where glycated protein is bound to the support and non-glycated protein is not substantially bound. Diagnostic devices and kits comprising the methods of the present invention are also provided.
    Type: Grant
    Filed: February 7, 2007
    Date of Patent: April 13, 2010
    Assignee: Scripps Laboratories, Inc.
    Inventors: Ralph P. McCroskey, Cameron E. Melton
  • Publication number: 20100081187
    Abstract: Methods of isolating highly sialylated recombinant vitamin K dependent proteins, particularly Factor IX, by chromatographic methods are described. The highly sialylated recombinant proteins are characterized. The improved Factor IX has at least 62% N-glycosylation with 3 or 4 sialic acid residues and improved bioavailability and pharmokinetic properties.
    Type: Application
    Filed: April 28, 2008
    Publication date: April 1, 2010
    Inventors: Michael J. Griffith, William N. Drohan, Marian J. Drohan
  • Patent number: 7667009
    Abstract: A method for purifying a modified major mite allergen obtained by the genetic recombination technique and a purified modified major mite allergen obtained by said method for purification are provided.
    Type: Grant
    Filed: April 14, 2004
    Date of Patent: February 23, 2010
    Assignee: Juridical Foundation the Chemo-Sero-Therapeutic Research Institute
    Inventors: Satoshi Koyanagi, Kenjiro Kawatsu, Toshio Murakami, Yoshinobu Miyatsu, Toshihiro Maeda, Hiroshi Mizokami
  • Patent number: 7662930
    Abstract: Various embodiments of the present invention are directed to multi-step systems and methods for target-molecule purification that employ column-chromatography-based and/or membrane-filtration-based polishing steps. In one described embodiment of the present invention, a target-protein-containing eluate having a high residual salt concentration is collected from a first chromatography column prepared with an affinity-chromatography resin, loaded onto a second chromatography column prepared with a cation-exchange resin, and eluted from the second cation-exchange column using a buffer in which a time-dependent pH gradient is established. In another described embodiment of the present invention, a partially purified target-protein-containing eluate is collected from a chromatography column and further purified by passing the target-protein-containing eluate through a salt-tolerant anion exchanger.
    Type: Grant
    Filed: December 6, 2006
    Date of Patent: February 16, 2010
    Assignee: AMGEN Inc.
    Inventor: Joe Xin Hua Zhou
  • Patent number: 7651848
    Abstract: A method for refolding a protein by mixing a protein solution with a refolding buffer at mixing conditions that approximate ideal mixing. The method can be carried out batch wise, in a fed-batch mode or continuously with on-line solubilization of inclusion bodies.
    Type: Grant
    Filed: April 3, 2007
    Date of Patent: January 26, 2010
    Assignee: Boehringer Ingelheim RCV GmbH & Co. KG
    Inventor: Robert Schlegl
  • Publication number: 20090324650
    Abstract: A method for the production of a purified extract of natural allergens comprising the steps of a) extracting a natural source of allergens comprising allergenic proteins to form an extract, b) purifying of said extract to remove non-protein components to form a purified extract c) denaturating said purified extract to form a purified denaturated extract, said purified denaturated extract comprising proteins, wherein the most abundant (w/w) proteins, forming together at least 60% (w/w) of all proteins, are at least two proteins, and all proteins represent at least 60% (w/w) of the dry weight of the purified denaturated extract and a method for the production of a purified extract of natural allergens comprising the steps of a) hydrolysing a denaturated allergen to form an allergen hydrolysate, b) purifying said allergen hydrolysate to remove peptides with a molecular weight above 10,000 Da and below 1,000 Da in order to obtain a purified hydrolysate where 70%, more preferably 80% of the peptides are betwe
    Type: Application
    Filed: June 28, 2007
    Publication date: December 31, 2009
    Inventors: Thierry Legon, Sabine Pirotton, Gael Placier, Gilles Kergoat
  • Patent number: 7632409
    Abstract: A displacement chromatography process and displacer compounds used in the process and having the general formula (I): wherein: each group R1, R2, R3, R?1, R?2, and R?3, independently may be selected from alkyl, aryl, and aralkyl, and in which a ring containing one or more quaternary nitrogen may be formed by any one or more of R1 and R2, R1 and R?1, R1 and R4, R4 and R?4, or R4 and R5; each R4, R?4, R5 and R?5 independently may be selected from alkyl, aryl, aralkyl and —(CH2)a—(CHY)b—(CH2)c—N+R1R2R3 An?, wherein R1, R2 and R3 are as defined above; each Y independently may be selected from —H, —OH, —OR6, halo, alkyl, aryl and aralkyl, wherein —R6 may be alkyl or —(CH2)a—(CHOH)b—(CH2)c—N+R1R2R3 An?, wherein R1, R2 and R3 are as defined above; each q and z independently may be any whole number from 0 to about 6, with the proviso that q+z is equal to or less than about 6; each a, b, and c independently may be any whole number from 0 to 2, with the proviso that the sum a+b+c in any fragment is at least 1; a
    Type: Grant
    Filed: October 23, 2006
    Date of Patent: December 15, 2009
    Assignee: SACHEM, Inc.
    Inventors: Charles Little, Victor van de Pas, Barry Haymore
  • Publication number: 20090306350
    Abstract: The invention relates to methods for purifying lactoferrin, stabilizing it in solution and improving its activity. In one embodiment of the present invention, it is provided methods for lactoferrin purification employing hydrophobic and/or hydrophilic adsorbent under specific conditions for maintaining or preserving lactoferrin protein stability. It is also provided a process to remove inhibitor of lactoferrin activity.
    Type: Application
    Filed: May 12, 2006
    Publication date: December 10, 2009
    Applicant: CREA BIOPHARMA INC.
    Inventors: Gerald Rowe, Hafida Aomari, Denis Petitclerc
  • Patent number: RE41555
    Abstract: This invention relates to the application of hydrophobic interaction chromatography combination chromatography to the purification of antibody molecular proteins.
    Type: Grant
    Filed: May 18, 2007
    Date of Patent: August 24, 2010
    Assignee: Glaxosmithkline LLC
    Inventors: Paula Shadle, John C. Erickson, Robert G. Scott, Thomas M. Smith
  • Patent number: RE41595
    Abstract: This invention relates to the application of hydrophobic interaction chromatography combination chromatography to the purification of antibody molecule proteins.
    Type: Grant
    Filed: March 13, 2009
    Date of Patent: August 31, 2010
    Assignee: GlaxoSmithKline LLC
    Inventors: Paul J. Shandle, John C. Erickson, Robert G. Scott, Thomas M. Smith