Separation Or Purification Patents (Class 530/344)
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Publication number: 20110098446Abstract: Process for the separation of a biomolecule containing at least one cationic group from a liquid medium containing said biomolecule, which comprises the use of a tetraphenylborate (TPB) salt.Type: ApplicationFiled: June 17, 2009Publication date: April 28, 2011Applicant: SOLVAY (SOCIETE ANONYME)Inventors: Roland Callens, Laurent Jeannin
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Patent number: 7928191Abstract: 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: GrantFiled: August 29, 2008Date of Patent: April 19, 2011Assignee: Fujifilm CorporationInventors: Koichi Minami, Yohsuke Takeuchi, Taisei Nishimi
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Publication number: 20110084203Abstract: A method and apparatus for conducting the rapid pyrolysis of peptides, proteins, polymers, and biological materials. The method can be carried out at atmospheric pressures and takes only about 5 to 30 seconds. The samples are cleaved at the C-terminus of aspartic acid. The apparatus employs a probe on which the sample is heated and digested components analyzed.Type: ApplicationFiled: February 16, 2009Publication date: April 14, 2011Inventors: Franco Basile, Shaofeng Zhang
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Patent number: 7915008Abstract: Changes in sialylation of cell surface or plasma proteins are often associated with various cancers and other disease conditions. Provided are methods of detecting biomarkers of conditions associated with a change of sialylation status. Sialylated peptides are first isolated from biological and other samples by loading onto titanium dioxide (TiO2) or zirconium dioxide (ZrO2) stationary phase under acidic conditions in a solution comprising at least 20% organic phase and at least about 6.5 mM of substituted aromatic carboxylic acid, or, alternatively, at least about 11 mM short chain, non-aromatic, hydroxylated carboxylic acid. Sialic acid containing proteins can then be eluted from loaded stationary phase material by exposure to an alkaline solution having pH of 9.0 or greater, preferably at least 10.5.Type: GrantFiled: April 27, 2007Date of Patent: March 29, 2011Assignee: Syddansk UniversitetInventor: Martin Rossel Larsen
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Publication number: 20110071274Abstract: The present invention refers to a method for binding a polycarboxylic acid to a solid phase. Further, the invention refers to a solid phase having a polycarboxylic acid immobilized thereto and methods of using the solid phase, e.g. for purifying His-tagged recombinant polypeptides.Type: ApplicationFiled: August 6, 2008Publication date: March 24, 2011Applicant: Max-Planck-Gesellschaft zur Foerderung der Wissenschaften e.V.Inventors: Dirk Goerlich, Steffen Frey
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Publication number: 20110070663Abstract: The present invention relates to a method for the purification and isolation of phosphorylated and glycosylated analytes using titanium dioxide particles.Type: ApplicationFiled: April 30, 2009Publication date: March 24, 2011Inventors: Joerg Von Hagen, Uwe Michelsen
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Publication number: 20110065900Abstract: The present invention relates to a method for removing at least one negatively charged substance from an aqueous liquid by contacting the liquid with a separation matrix comprising a plurality of polyallylamine ligands, comprising binding said negatively charged substance to said ligands under conditions where the ionic strength of the aqueous liquid applied to the chromatography resin ?0.25 M NaCl.Type: ApplicationFiled: May 29, 2009Publication date: March 17, 2011Applicant: GE HEALTHCARE BIO-SCIENCE ABInventors: Bo-Lennart Johansson, Ulrika Karlsson, Jean-Luc Maloisel
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Publication number: 20110065897Abstract: 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: ApplicationFiled: April 9, 2009Publication date: March 17, 2011Inventor: Christian Feckler
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Publication number: 20110065647Abstract: The presently described subject matter relates to isolated spider venom peptides, which are used as potent and selective ion channel blockers, and to a composition and methods for treatment of pain.Type: ApplicationFiled: September 14, 2010Publication date: March 17, 2011Applicant: BIOSEARCH (2007) LTD.Inventors: Alon MEIR, Ronit Simcha CHERKI, Ela KOLB, Yael LANGUT, Nissim BAJAYO
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Publication number: 20110053242Abstract: The invention provides methods for isolating a modified peptide from a complex mixture of peptides, the method comprising the steps of: (a) obtaining a proteinaceous preparation from an organism, wherein the preparation comprises modified peptides from two or more different proteins; (b) contacting the preparation with at least one immobilized modification-specific antibody; and (c) isolating at least one modified peptide specifically bound by the immobilized modification-specific antibody in step (b). The method may further comprise the step of (d) characterizing the modified peptide isolated in step (c) by mass spectrometry (MS), tandem mass spectrometry (MS-MS), and/or MS3 analysis, or the step of (e) utilizing a search program to substantially match the spectra obtained for the modified peptide during the characterization of step (d) with the spectra for a known peptide sequence, thereby identifying the parent protein(s) of the modified peptide.Type: ApplicationFiled: June 28, 2007Publication date: March 3, 2011Inventors: John Rush, Hui Zhang, Xiangming Zha, Michael J. Comb, Yi Tan
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Publication number: 20110045538Abstract: Provided is a peptide containing a variable region and improved in production efficiency. The peptide contains a variable region to which an antigen-binding site is to be formed and has an amino acid sequence expressing a specific adsorption function to a solid phase at a site closer to the C-terminal than a heavy-chain variable region or at a site closer to the C-terminal than a light-chain variable region.Type: ApplicationFiled: February 12, 2009Publication date: February 24, 2011Inventors: Yoichi Kumada, Michimasa Kishimoto, Yuki Shiritani, Kyoko Hamasaki N/A, Takuhito Ohse, Mitsuyasu Koike
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Publication number: 20110036133Abstract: The present invention relates to a process to purify enzymatically digested heparin-derived protein hydrolysate (peptone) comprising the step of passing the peptone through a nanofilter at a temperature of about ambient to about 130° F. and a pressure of about ambient to about 360 psi resulting in peptone concentrate.Type: ApplicationFiled: April 15, 2009Publication date: February 17, 2011Inventors: Timothy James Hadden, Gary Merle Kurtz
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Publication number: 20110039765Abstract: The present invention is a method for isolating bioactive molecules secreted by probiotic bacteria such as Lactobacillus rhamnosus, and methods for using such bioactive molecules to decrease replication of human immunodeficiency virus, expression of inflammatory cytokines and chemokines, expression of vasoendothelial growth factor, Erk1/Erk2 activation, and to inhibit HIV transmission.Type: ApplicationFiled: March 9, 2009Publication date: February 17, 2011Inventor: Ruth I. Connor
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Patent number: 7884187Abstract: Methods for analyzing, selecting, characterizing or classifying compositions of a co-polymer, e.g., glatiramer acetate are described. The methods entail analysis of pyro-glutamate in the composition, and, in some methods, comparing the amount of pyro-glutamate present in a composition to a reference standard.Type: GrantFiled: September 15, 2010Date of Patent: February 8, 2011Assignee: Momenta Pharmaceuticals, Inc.Inventors: Xiangping Zhu, Zachary Shriver, Yanjie Jiang, Corinne Bauer, James Eric Anderson, Peter James Ahern
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Patent number: 7879976Abstract: The invention relates to a method for stabilizing an aqueous protein solution against exogenous stress and to the use of a container for stabilizing an aqueous protein solution.Type: GrantFiled: April 25, 2008Date of Patent: February 1, 2011Assignee: Hoffmann-La Roche Inc.Inventors: Wolfgang Friess, Sylvia Kiese, Hanns-Christian Mahler, Astrid Pappenberger
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Publication number: 20110015373Abstract: The present invention relates to a method of separating or extracting phosphorylated amino acids, peptides or proteins with a molecularly imprinted polymer and to the preparation of said molecularly imprinted polymer as well as use of a molecularly imprinted polymer for separating or extracting phosphorylated amino acids, peptides or proteins.Type: ApplicationFiled: November 11, 2008Publication date: January 20, 2011Applicant: MIP TECHNOLOGIES ABInventors: Borje Sellergren, Marco Emgenbroich, Andrew J. Hall
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Publication number: 20100331522Abstract: Lysing may include agitating a specimen in a chamber along with a medium that includes a particulate lysing material that has an affinity for a biological material. Lysing material may include beads or other material which may be coated that facilitates binding. The medium may include a fluid with a high salt or low pH level. The biological material may be eluted by lowering a concentration of salt or increasing a pH level. Lysing materials with two or more different affinities may be employed. Heating may be used. Lysing may be performed in a flow through apparatus.Type: ApplicationFiled: June 24, 2010Publication date: December 30, 2010Inventors: Bruce Irvine, Robert W. Doebler, Barbara Erwin, Ryan P. Talbot, Angelika Brigitte Niemz
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Publication number: 20100330680Abstract: The present invention provides methods for enhancing the fragmentation of peptides for mass spectrometry by modifying the peptides with a tagging reagent containing a functional group, such as a tertiary amine, having a greater gas-phase basicity than the amide backbone of the peptide. These high gas-phase basicity functional groups are attached to a peptide by reacting the tagging reagent to one or more available carboxylic acid groups of the peptide. Linking these high gas-phase functional groups to the peptides leads to higher charge state ions from electrospray ionization mass spectrometry (ESI-MS), which fragment more extensively during fragmentation techniques, particularly non-ergodic fragmentation techniques such as electron capture dissociation (ECD) and electron transfer dissociation (ETD).Type: ApplicationFiled: April 14, 2010Publication date: December 30, 2010Inventors: Brian L. Frey, April L. Jue, Casey J. Krusemark, Lloyd M. Smith, Joshua J. Coon
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Publication number: 20100317827Abstract: The invention relates, interalia, to the field of purification of peptides, notably cyclic or non-cyclic peptides their analogs or derivatives thereof. More particularly, the invention relates to a simplified and optimized purification process of cyclic peptides from a composition comprising the said peptide and at least one related impurity by chromatographic procedures enabling high yields, selectivity and purity of the desired end product. The improved process is particularly useful for the preparation of eptifibatide, exenatide, atosiban, nesiritide and their respective derivatives and analogs. The polypeptides are prepared in high purity of at least about 96%, and preferably at least about 99%.Type: ApplicationFiled: March 26, 2008Publication date: December 16, 2010Applicant: BIOCON LIMITEDInventors: Nitesh Dave, Krishnamurthy Venkatesan, Ramprabu Nagarajan, Harish Iyer
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Publication number: 20100311947Abstract: A palladatepalladium-promoted hydrolytic polypeptide cleavage process which selectively cleaves the polypeptide at a Cys-His cleavage site comprising solubilizing the polypeptide in a reaction mixture comprised of a palladatepalladium promoter dissolved in a high-concentration acidic organic acid solvent.Type: ApplicationFiled: June 7, 2010Publication date: December 9, 2010Applicant: MEDTRONIC, INC.Inventors: Jin Seog Seo, Daniel Strydom, Barton Holmquist
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Publication number: 20100310877Abstract: This invention provides emulsions and adhesives comprising proteins that can be isolated from a variety of sources including renewable plant biomass, and methods of making and using such emulsions and adhesives.Type: ApplicationFiled: March 8, 2010Publication date: December 9, 2010Inventors: Anthony A. Parker, Joseph J. Marcinko
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Publication number: 20100304493Abstract: The present invention relates to the selective enrichment of post-translationally modified proteins and/or peptides from complex samples by combining a particular protein/peptide labeling and fractionation strategy with specific chemical and/or enzymatic reactions targeting the post-translational modification to be analyzed. More specifically, the invention relates to methods for the enrichment and/or separation of phospho-proteins and/or -peptides, and particularly for the discrimination between different subsets of phospho-proteins and/or -peptides in complex samples.Type: ApplicationFiled: November 17, 2008Publication date: December 2, 2010Applicant: KONINKLIJKE PHILIPS ELECTRONICS N.V.Inventors: Ralf Hoffmann, Hugo M. Visser, Edwin P. Romijn
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Publication number: 20100297734Abstract: The application discloses a fusion tag comprising an affinity tag and a polypeptide comprising one or more EF hand motif(s). Preferably, said fusion tag comprises a polyhistidine tag, one or more EF hand motif(s) of calmodulin and a thrombin cleavage site. Methods of using said fusion tag to purify a polypeptide of interest are also disclosed.Type: ApplicationFiled: October 10, 2008Publication date: November 25, 2010Applicant: University Health NetworkInventors: Andrew J. McCluskey, Gregory M.K. Poon, Jean Gariépy
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Publication number: 20100291629Abstract: The invention concerns the use of deleucocytation filters for defensin purification. More precisely, the invention concerns a method for purifying defensins, including the following steps: passing a blood sample on a deleucocytation filter; detaching the cells retained on the deleucocytation filter, inducing exocytosis of the defensins by those cells.Type: ApplicationFiled: March 27, 2007Publication date: November 18, 2010Applicant: ETABLISSEMENT FRANCAIS DU SANGInventors: Chantal Fournier-Wirth, Joliette Coste
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Publication number: 20100292440Abstract: It is an object of the present invention to provide novel binding molecules for factor VIII and factor VIII-like proteins. Preferred binding molecules of the present invention exhibit not only distinct characteristics for binding of the target factor VIII polypeptides but also specific and desirable characteristics for release (elution) of the target polypeptides. Especially preferred binding molecules according to the invention are short polypeptide sequences, characterized by a stable loop structure.Type: ApplicationFiled: January 22, 2010Publication date: November 18, 2010Applicant: Dyax Corp.Inventors: Jinan Yu, M. Daniel Potter, Brian D. Kelley, Jeffrey S. Deetz, James E. Booth, Marilous Potter
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Publication number: 20100286070Abstract: The present invention relates to an affinity tag especially useful for human applications. The invention further includes methods for preparing fusion molecules, as well as compositions and reaction mixtures which contain said fusion molecules, nucleic acid molecules which encode these fusion molecules and recombinant host cells which contain these nucleic acid molecules.Type: ApplicationFiled: September 15, 2008Publication date: November 11, 2010Inventors: Gert Verheyden, Fons Bosman
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Publication number: 20100285596Abstract: The invention provides methods of isolating, purifying, analyzing and/or detecting, functionalized macromolecules, e.g., peptides, phosphopeptides, polypeptides, proteins, oligonucleotides, or phospholipids in a sample, e.g., a biological mixture, using solid phase extraction with an alumina sorbent packed in a micro-elution plate.Type: ApplicationFiled: September 5, 2008Publication date: November 11, 2010Applicant: WATERS TECHNOLOGIES CORPORATIONInventors: Ying Qing Yu, Martin Gilar
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Publication number: 20100273983Abstract: A method is provided for purifying peptides by selective precipitation of contaminating proteins, such as host cell proteins and cleaved fusion partners. Also provided is a method of cleaving fusion proteins in cell lysates.Type: ApplicationFiled: April 4, 2008Publication date: October 28, 2010Applicant: The University of QueenslandInventors: Waltraud Kaar, Robert John Falconer, Anton Peter Jacob Middelberg, Belinda Maree Hartmann
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Patent number: 7820619Abstract: The peptides and derivative metapeptides based upon natural antimicrobial peptides have potent and broad spectrum activity against pathogens exhibiting multiple antibiotic resistance. Specific peptides can also potentiate the antimicrobial functions of leukocytes, such as neutrophils. In addition, they exhibit lower inherent mammalian cell toxicities than conventional antimicrobial peptides, and overcome problems of toxicity, immunogenicity, and shortness of duration of effectiveness due to biodegradation, retaining activity in plasma and serum. The peptides and derivative metapeptides exhibit rapid microbicidal activities in vitro, can be used to potentiate conventional antimicrobial agents, to potentiate other antimicrobial peptides, and are active against many organisms that exhibit resistance to multiple antibiotics currently in existence.Type: GrantFiled: August 25, 2000Date of Patent: October 26, 2010Assignee: Los Angeles Biomedical Research Institute at Harbor-UCLA Medical CenterInventors: Michael R. Yeaman, Alexander J. Shen
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Patent number: 7820800Abstract: 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: GrantFiled: November 4, 2004Date of Patent: October 26, 2010Assignee: Ares Trading S.A.Inventors: Mara Rossi, Thierry Ziegler, Laure Valognes
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Publication number: 20100267999Abstract: A method for producing a microbial growth stimulant (MGS) from a plant biomass is described. In one embodiment, an ammonium hydroxide solution is used to extract a solution of proteins and ammonia from the biomass. Some of the proteins and ammonia are separated from the extracted solution to provide the MGS solution. The removed ammonia can be recycled and the proteins are useful as animal feeds. In one embodiment, the method comprises extracting solubles from pretreated lignocellulosic biomass with a cellulase enzyme-producing growth medium (such T. reesei) in the presence of water and an aqueous extract.Type: ApplicationFiled: April 19, 2010Publication date: October 21, 2010Inventors: Ming Woei Lau, Bruce Dale
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Publication number: 20100249371Abstract: The present invention provides simple, cost effective, rapid, and scalable at industrial scale and provide high purity and yield of Echinocandin-type compounds at low cost as compared to prior art. Moreover the process allows for the removal of impurities by using economical salt-adsorbent complex and provide highly purified Echinocandin type compounds which is highly improved in terms of purity and sufficient for further processing to obtain an active pharmaceutical ingredient such as, the antifungals caspogungin, anidulafungin, and micafungin.Type: ApplicationFiled: March 23, 2010Publication date: September 30, 2010Inventors: Menka GURNANI, Rajkumar Maurya
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Patent number: 7803774Abstract: Compounds that modulate natural ? amyloid peptide aggregation are provided. The modulators of the invention comprise a peptide, preferably based on a ? amyloid peptide, that is comprised entirely of D-amino acids. Preferably, the peptide comprises 3-5 D-amino acid residues and includes at least two D-amino acid residues independently selected from the group consisting of D-leucine, D-phenylalanine and D-valine. In a particularly preferred embodiment, the peptide is a retro-inverso isomer of a ? amyloid peptide, preferably a retro-inverso isomer of A?17-21. In certain embodiments, the peptide is modified at the amino-terminus, the carboxy-terminus, or both. Preferred amino-terminal modifying groups alkyl groups. Preferred carboxy-terminal modifying groups include an amide group, an acetate group, an alkyl amide group, an aryl amide group or a hydroxy group.Type: GrantFiled: November 15, 2004Date of Patent: September 28, 2010Assignee: Praecis Pharmaceuticals, Inc.Inventors: Mark A. Findeis, Kathryn Phillips, Gary L. Olsen, Christopher Self
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Publication number: 20100234567Abstract: The object of the present invention is a procedure for the distribution, separation and purification in aqueous solution of recombinant proteins, based on the utilization of polypeptides with choline affinity. The invention is based on a phenomenon consisting of that two aqueous solutions with determinated components can be mixed, being distributed finally in two phases with different density. The fusionated proteins to said polypeptides with choline affinity are preferably located in one of the phases, while most of the cell extract proteins tend to go to the opposite phase. After a series of washings for removing the rest of the not desired material, this location can be inverted through the addition of a soluble molecule with affinity by the polypeptide fusionated to the protein of interest. This procedure allows modulating at convenience the presence of the protein or polypeptide of interest in one phase or another, possibiliting its purification with a high yield and purity grade.Type: ApplicationFiled: March 12, 2010Publication date: September 16, 2010Applicant: BIOMEDAL, S.L.Inventors: Jesús M. SANZ MORALES, Beatriz Maestro Garcia-Donas, Miguel Arevalo Rodriguez, Isabel Velasco Umpierrez, Angel Cebolla Ramirez
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Patent number: 7795405Abstract: 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: GrantFiled: January 29, 2007Date of Patent: September 14, 2010Assignee: Guild Associates, Inc.Inventor: Augustine DiNovo
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Publication number: 20100228006Abstract: The present invention relates to a process for purifying lipopeptides. More particular, the invention provides an improved method for purifying daptomycin.Type: ApplicationFiled: February 19, 2010Publication date: September 9, 2010Applicant: AXELLIA PHARMACEUTICALS APSInventors: Martin Mansson, Eli Karin Dale, Sissel Hauge, Carsten Overballe-Petersen, Kjersti Aastorp Hirth, Dennis Brian Hansen
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Publication number: 20100222252Abstract: The present invention provides a deshydroxy vancomycin compound,a method of its preparation and a pharmaceutical composition comprising a pharmaceutically effective amount of the deshydroxy vancomycin and the use of the said composition in the preparation of drugs for the treatment of susceptible bacteria infections. The method includes the following steps: (1) preparing a concentrated vancomycin solution containing the deshydroxy vancomycin by fermentations of Amycolatopsis Orientalis with Deposit No. CGMCCNO.1183; (2) separating and purifing the concentrated vancomycin solution to obtain a refined filtrate of vancomycin hydrochloride containing the deshydroxy vancomycin by column chromatography; and (3) further separating and purifing the refined filtrate to obtain the deshydroxy vancomycin by chromatography.Type: ApplicationFiled: August 25, 2008Publication date: September 2, 2010Inventors: Bingxiang Xu, Haisong Xie, Huan Yu, Wei Mao, Weidong Ye
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Publication number: 20100197009Abstract: The application relates to antibodies which recognize the AviTag™ peptide of sequence MSGLNDIFEAQKIEWHE (SEQ ID No. 1) and to fragments thereof which recognize SEQ ID No. 1, wherein said antibodies or said fragments thereof recognize polypeptides containing SEQ ID No. 1 at their NH2 terminus and polypeptides containing SEQ ID No. 1 at their COOH terminus. The application further relates to a method for sorting target cells presenting on their surface a surface marker from a mixed cell population comprising the steps of: a) incubating said mixed cell population with a tagged adapter which binds to said surface marker of said target cells, wherein said adapter is bound to an antibody which recognizes said tag, and wherein said antibody is immobilized on a solid support. b) collecting said target cells.Type: ApplicationFiled: July 11, 2008Publication date: August 5, 2010Applicant: INSERM(Institut National de la Sante et de la Recherche Medicale)Inventors: Francois Lang, Karine Bernardeau, Regis Bouquie, Nathalie Labarriere
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Publication number: 20100190958Abstract: The new pure vancomycin hydrochloride substantially free of impurities known in commercially available products is described. The term “substantially free of impurities” designates a purity of vancomycin hydrochloride between about 97% and about 99%, particularly between about 98% and about 99%, preferably about 99%, as determined by HPLC analytical method as directed in U.S.P., NF 27th revision, 22 (2004). The new pure vancomycin hydrochloride (vancomycin B hydrochloride) contains less than 0.7% of total impurities, namely, only one impurity exceeds 0.3%. The new process for the purification of crude vancomycin by displacement chromatography is described by which the desired pure antibiotic according to the present invention is produced, based on the finding that high purity of the vancomycin hydrochloride is obtained using low selected pH values of the mobile phase between 3.9 and 4.2.Type: ApplicationFiled: December 5, 2005Publication date: July 29, 2010Applicant: LEK PHARMACEUTICAL D.D.Inventors: Rok Grahek, Andrej Bastarda
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Publication number: 20100184687Abstract: Method for purifying a glucagon-like peptide by reversed phase high performance liquid chromatography.Type: ApplicationFiled: March 17, 2010Publication date: July 22, 2010Applicant: Novo Nordisk A/SInventors: Arne Staby, Camilla Kornbeck, Dorte Lunøe Dünweber, Hanne Christensen, Ole Schou
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Publication number: 20100167374Abstract: The present invention relates to a chromatographic method of separating biological material comprising, providing chromatographic media comprising inorganic oxide particles having an average diameter of about 2 microns or less and an average pore diameter of 300 ? or more; applying a solvent comprising said biological material to said media, wherein said biological material is reversibly bonded to said media; and eluting said biological material from said media with a solvent in less than about 2 minutes for biological material having a molecular weight of less than about 100,000 Daltons.Type: ApplicationFiled: February 21, 2008Publication date: July 1, 2010Inventors: Reno T. Nguyen, Scott Anderson, Ian Chappell
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Publication number: 20100160606Abstract: A process of purifying copolymer peptides such as COP-1 polypeptides by ultrafiltration can be improved by treating the polypeptide solution with an acid before, or during the early stages of, the ultrafiltration. By adding the acid and/or forming an acid addition salts of the polypeptide before ultrafiltration is conducted permits for faster ultrafiltration. Likewise, adding the acid in the ultrafiltration process but before polypeptide precipitation or clogging occurs can also improve the efficiency/convenience of the ultrafiltration step.Type: ApplicationFiled: December 23, 2009Publication date: June 24, 2010Inventor: Jordy Luten
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Publication number: 20100160605Abstract: 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: ApplicationFiled: December 17, 2009Publication date: June 24, 2010Applicant: TOSOH CORPORATIONInventors: Katsuo KOMIYA, Koji NAKAMURA
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Publication number: 20100143396Abstract: The invention relates to a method for the preparation of a stabilized cross-linked oligomer of amyloid beta using a near-zero length bifunctional cross-linking agent for use as an immunogen for the generation of antibodies for the treatment of Alzheimer's Disease and other conditions related to abnormal amyloid beta aggregation. A preferred bifunctional cross-linking agent is 1,5-difluoro-2,4-dinitrobenzene (DFDNB).Type: ApplicationFiled: June 26, 2006Publication date: June 10, 2010Inventors: Karen M. Grimm, Joseph G. Joyce, Xiaoping Liang, Denise Nawrocki
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Publication number: 20100144045Abstract: The invention relates to the use of compounds as new chiral selectors for separating the optical or enantiomeric isomers of a compound, wherein the chiral selector comprises at least one compound of formula (I): and at least one metal ion, for example Cu2+, Ni2+, Zn2+, Cd2+ or Co2+.Type: ApplicationFiled: March 13, 2008Publication date: June 10, 2010Inventors: Eric Peyrin, Jean-Luc Decout, Corrine Ravelet, Isabelle Henriette Baussanne
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Publication number: 20100129889Abstract: An affinity matrix comprising a base matrix containing biotin; and a fusion protein attached to the base matrix, wherein the fusion protein contains a matrix binding element capable of binding to the base matrix via biotin and a target binding element capable of binding, or being bound by, at least one target component.Type: ApplicationFiled: August 31, 2007Publication date: May 27, 2010Applicant: INNOVATIVE PURIFICATION TECHNOLOGIES PTY LTDInventor: Jens Sommer-Knudsen
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Publication number: 20100125128Abstract: Phosphorylated peptides are extracted from digests of biological liquids and other peptide mixtures by fractionation on ceramic hydroxyapatite. The ceramic hydroxyapatite is readily usable in a centrifuge, allowing for rapid fractionations of a large number of small volume samples, and accordingly high throughput.Type: ApplicationFiled: November 9, 2009Publication date: May 20, 2010Applicant: BIO-RAD LABORATORIES, INC.Inventors: Ning Liu, Katrina Academia, Aran Paulus, Tim Wehr, John A. Walker, II, Steve Freeby
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Patent number: 7718598Abstract: This invention relates to methods for preparing cyclic peptides and peptidomimetic compounds in solution and bound to solid supports, and to cyclic peptide or peptidomimetic libraries for use in drug screening programmes. In particular, the invention relates to a generic strategy for synthesis of cyclic peptides or peptidomimetics that enables the efficient synthesis under mild conditions of a wide variety of desired compounds. Two approaches were evaluated for their improvements in solution and solid phase synthesis of small cyclic peptides: positioning reversible N-amide substituents in the sequence; and applying native ligation chemistry in an intramolecular sense. Systematic investigation of the effects of preorganizing peptides prior to cyclisation by using peptide cyclisation auxiliaries, and developing new linkers and peptide cyclisation auxiliaries to aid cyclic peptide synthesis gives surprising improvements in both yields and purity of products compared to the prior art methods.Type: GrantFiled: September 24, 1999Date of Patent: May 18, 2010Assignee: The University of QueenslandInventors: Mark Leslie Smythe, Wim Denis Frans Meutermans
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Patent number: 7713926Abstract: The peptide production method of the present invention produces a peptide (SEQ ID NO: 1) of a protein from Plasmodium falciparum, which is effective as a malaria vaccine. The method produces the peptide of SEQ ID NO: 1 by linking the fragments (i) through (v) shown below: (v) Asn-Asn-Asp-Xaa (SEQ ID NO: 2); (iv) Asp-Phe-Lys-Thr-Pro (SEQ ID NO: 3); (iii) Asn-Lys-Thr-Tyr-Asp-Leu (SEQ ID NO: 4); (ii) Phe-Tyr-Asn-Ser-Glu (SEQ ID NO: 5); and (i) Xaa-Ala-Ser-Glu (SEQ ID NO: 6), where ‘Xaa’ in (i) and (v) represents zero or any arbitrary number of amino acid residues.Type: GrantFiled: September 28, 2005Date of Patent: May 11, 2010Assignee: National University Corporation Gunma UniversityInventors: Hiroyuki Oku, Kazuto Omi, Keisuke Kuriyama, Jyunya Yamamoto, Keiichi Yamada, Ryoichi Katakai, Kumiko Sato, Mamoru Suzuki, Shin-ichiro Kawazu, Shigeyuki Kano
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Patent number: 7696313Abstract: The compounds of the invention are modified forms of therapeutic agents. A typical prodrug compound of the invention comprises a therapeutic agent, an oligopeptide having an isoleucine residue, a stabilizing group and, optionally, a linker group. The prodrug is cleavable by an enzyme associated with the target cell. Methods of making and using the compounds are also disclosed.Type: GrantFiled: January 16, 2008Date of Patent: April 13, 2010Assignee: Medarex, Inc.Inventors: Lesley B. Pickford, Sanjeev Gangwar, Thomas J. Lobl, Matthew H. Nieder, Geoffrey T. Yarranton