CN1211485C - 生产重组白蛋白的方法 - Google Patents
生产重组白蛋白的方法 Download PDFInfo
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- CN1211485C CN1211485C CNB008032920A CN00803292A CN1211485C CN 1211485 C CN1211485 C CN 1211485C CN B008032920 A CNB008032920 A CN B008032920A CN 00803292 A CN00803292 A CN 00803292A CN 1211485 C CN1211485 C CN 1211485C
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Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
GB9902000D0 (en) * | 1999-01-30 | 1999-03-17 | Delta Biotechnology Ltd | Process |
US6926898B2 (en) | 2000-04-12 | 2005-08-09 | Human Genome Sciences, Inc. | Albumin fusion proteins |
ITBO20010426A1 (it) * | 2001-07-06 | 2003-01-06 | Alfa Wassermann Spa | Processo per la purificazione di proteine farmacologicamente attive mediante cromatografia in scambio cationico |
US7176278B2 (en) | 2001-08-30 | 2007-02-13 | Biorexis Technology, Inc. | Modified transferrin fusion proteins |
ES2500918T3 (es) | 2001-12-21 | 2014-10-01 | Human Genome Sciences, Inc. | Proteínas de fusión de albúmina e interferón beta |
GB0202633D0 (en) * | 2002-02-05 | 2002-03-20 | Delta Biotechnology Ltd | Stabilization of protein preparations |
JP2005516607A (ja) | 2002-02-07 | 2005-06-09 | デルタ バイオテクノロジー リミテッド | Hiv阻害タンパク質 |
SE526227C2 (sv) * | 2002-05-15 | 2005-08-02 | North China Pharmaceutical Group | Metod för rening av rekombinant humant serumalbumin |
GB0217033D0 (en) | 2002-07-23 | 2002-08-28 | Delta Biotechnology Ltd | Gene and polypeptide sequences |
GB0304576D0 (en) | 2003-02-28 | 2003-04-02 | Lonza Biologics Plc | Protein a chromatography |
ATE539086T1 (de) | 2003-12-03 | 2012-01-15 | Monika Kroez | Interleukin-11-fusionsproteine |
US9057061B2 (en) | 2003-12-23 | 2015-06-16 | Novozymes Biopharma Dk A/S | Gene expression technique |
GB0329722D0 (en) * | 2003-12-23 | 2004-01-28 | Delta Biotechnology Ltd | Modified plasmid and use thereof |
GB0329681D0 (en) | 2003-12-23 | 2004-01-28 | Delta Biotechnology Ltd | Gene expression technique |
WO2006066595A2 (en) * | 2004-12-22 | 2006-06-29 | Novozymes A/S | Recombinant production of serum albumin |
WO2007063129A2 (en) * | 2005-12-02 | 2007-06-07 | Novozymes A/S | Insolation of peptides , polypeptides and proteins |
JP2007284425A (ja) * | 2006-03-20 | 2007-11-01 | Nokodai Tlo Kk | タンパク質の精製方法 |
US9139611B2 (en) | 2006-07-13 | 2015-09-22 | Novozymes Biopharma Dk A/S | Process for preparing particles of proteinaceous material |
WO2008012629A2 (en) | 2006-07-24 | 2008-01-31 | Biorexis Pharmaceutical Corporation | Exendin fusion proteins |
WO2008019368A2 (en) | 2006-08-07 | 2008-02-14 | Teva Biopharmaceuticals Usa, Inc. | Albumin-insulin fusion proteins |
SG10201405420QA (en) * | 2007-02-02 | 2014-10-30 | Globeimmune Inc | Methods for producing yeast-based vaccines |
CA2695830A1 (en) | 2007-08-08 | 2009-02-12 | Novozymes Biopharma Dk A/S | Transferrin variants and conjugates |
EP2261661A4 (en) | 2008-03-31 | 2011-04-20 | Sekisui Medical Co Ltd | CLEANED SERUM ALBUMIN AND IMMUNOLOGY MEASUREMENT PROCESS |
CN101684459B (zh) * | 2008-09-22 | 2012-01-25 | 上海普天欣生物技术有限公司 | CehA突变体蛋白、基因、重组载体及其用途和制备方法 |
CN101747437B (zh) | 2008-12-10 | 2012-09-26 | 浙江日升昌药业有限公司 | 凋亡素-ec-sod羧基末端蛋白转导域融合蛋白 |
EP3243835B1 (en) | 2009-02-11 | 2024-04-10 | Albumedix Ltd | Albumin variants and conjugates |
AU2010215959A1 (en) | 2009-02-20 | 2011-08-04 | Ventria Bioscience | Cell culture media containing combinations of proteins |
CN102405279B (zh) | 2009-04-09 | 2015-10-21 | 塞尔卡有限公司 | 改善单细胞克隆的方法 |
DK2427486T3 (en) * | 2009-05-07 | 2015-05-26 | Novozymes Biopharma Dk As | A process for purifying albumin |
CN101691581B (zh) * | 2009-06-25 | 2012-10-03 | 南京农业大学 | 染色体无标记随机整合载体pUTTns及其应用 |
US8129139B2 (en) | 2009-07-13 | 2012-03-06 | Allergan, Inc. | Process for obtaining botulinum neurotoxin |
CN101690801B (zh) | 2009-10-26 | 2012-08-01 | 上海交通大学 | 白细胞介素-1受体拮抗剂的用途及其药物组合物 |
CA2776241A1 (en) | 2009-10-30 | 2011-05-05 | Novozymes Biopharma Dk A/S | Albumin variants |
WO2011124718A1 (en) | 2010-04-09 | 2011-10-13 | Novozymes A/S | Albumin derivatives and variants |
NZ603289A (en) * | 2010-04-29 | 2014-07-25 | Baxter Int | Purification method for divalent cation binding proteins on anion exchange resin |
US20130225496A1 (en) | 2010-11-01 | 2013-08-29 | Novozymes Biopharma Dk A/S | Albumin Variants |
CN102127164B (zh) * | 2010-12-20 | 2013-01-30 | 武汉禾元生物科技有限公司 | 一种从水稻种子中提取重组人血清白蛋白的方法 |
CN102532254B (zh) | 2010-12-24 | 2015-06-24 | 武汉禾元生物科技股份有限公司 | 一种从水稻种子中分离纯化重组人血清白蛋白的方法 |
GB2491006A (en) | 2011-05-05 | 2012-11-21 | Novozymes Biopharma Uk Ltd | Albumin variants |
CA2838964C (en) * | 2011-07-05 | 2021-07-13 | Novozymes Biopharma Dk A/S | Albumin formulation and use |
EP2780364A2 (en) | 2011-11-18 | 2014-09-24 | Eleven Biotherapeutics, Inc. | Proteins with improved half-life and other properties |
EP2788033B1 (en) * | 2011-12-05 | 2017-05-31 | Factor Bioscience Inc. | Methods and products for transfecting cells |
RS63244B1 (sr) | 2011-12-16 | 2022-06-30 | Modernatx Inc | Kompozicije modifikovane mrna |
US9944691B2 (en) | 2012-03-16 | 2018-04-17 | Albumedix A/S | Albumin variants |
US9283287B2 (en) | 2012-04-02 | 2016-03-15 | Moderna Therapeutics, Inc. | Modified polynucleotides for the production of nuclear proteins |
WO2013151664A1 (en) * | 2012-04-02 | 2013-10-10 | modeRNA Therapeutics | Modified polynucleotides for the production of proteins |
US9303079B2 (en) | 2012-04-02 | 2016-04-05 | Moderna Therapeutics, Inc. | Modified polynucleotides for the production of cytoplasmic and cytoskeletal proteins |
US10501513B2 (en) * | 2012-04-02 | 2019-12-10 | Modernatx, Inc. | Modified polynucleotides for the production of oncology-related proteins and peptides |
CN102952836A (zh) * | 2012-11-02 | 2013-03-06 | 浙江海正药业股份有限公司 | 重组人长效白介素1受体拮抗剂融合蛋白的纯化方法 |
US20140128326A1 (en) | 2012-11-08 | 2014-05-08 | Novozymes Biopharma Dk A/S | Albumin variants |
CN103880947B (zh) | 2012-12-21 | 2016-01-13 | 武汉禾元生物科技股份有限公司 | 一种分离纯化高纯度重组人血清白蛋白的层析方法 |
RU2663587C2 (ru) * | 2013-03-06 | 2018-08-07 | ГЛЭКСОСМИТКЛАЙН ЭлЭлСи | Клетки-хозяева и способы использования |
WO2014137903A2 (en) | 2013-03-08 | 2014-09-12 | Genzyme Corporation | Integrated continuous manufacturing of therapeutic protein drug substances |
SI3016970T1 (sl) | 2013-07-04 | 2019-08-30 | Glykos Finland Oy | Nitaste glivične celice brez O-manoziltransferaze in postopki za uporabo le-teh |
JP6306700B2 (ja) | 2013-11-01 | 2018-04-04 | ユニバーシティ オブ オスロUniversity of Oslo | アルブミン改変体及びその使用 |
TWI671312B (zh) | 2014-01-17 | 2019-09-11 | 美商健臻公司 | 無菌層析法及製法 |
TWI709569B (zh) | 2014-01-17 | 2020-11-11 | 美商健臻公司 | 無菌層析樹脂及其用於製造方法的用途 |
US9938319B2 (en) * | 2014-04-23 | 2018-04-10 | Alexion Pharmaceuticals, Inc. | Egg white processing |
WO2016012468A1 (en) | 2014-07-21 | 2016-01-28 | Novartis Ag | Production of glycoproteins with mammalian-like n-glycans in filamentous fungi |
EP3240798B8 (en) * | 2015-01-01 | 2020-03-25 | Shilpa Medicare Limited | Novel method for efficient purification of human serum albumin |
EP3543339A1 (en) | 2015-02-13 | 2019-09-25 | Factor Bioscience Inc. | Nucleic acid products and methods of administration thereof |
CA2979397A1 (en) | 2015-03-12 | 2016-09-15 | Board Of Trustees Of Michigan State University | Compositions and methods for measuring c-peptide binding and diagnosing immune-mediated diseases |
WO2016207730A1 (en) | 2015-06-22 | 2016-12-29 | The University Of Oslo | Targeting of vaccine antigen to an intracellular compartment |
CN105037487B (zh) * | 2015-08-12 | 2017-03-22 | 山东泰邦生物制品有限公司 | 一种人血白蛋白的制备方法 |
BR112018003179A2 (pt) | 2015-08-20 | 2018-09-25 | Albumedix As | conjugados e variantes de albumina |
CA3005953A1 (en) | 2015-12-22 | 2017-06-29 | Albumedix Ltd | Improved protein expression strains |
CN116115629A (zh) | 2016-08-17 | 2023-05-16 | 菲克特生物科学股份有限公司 | 核酸产品及其施用方法 |
KR102662031B1 (ko) | 2016-10-04 | 2024-05-03 | 알부메딕스 리미티드 | 재조합 효모-유래 혈청 알부민의 용도 |
WO2018096396A1 (en) | 2016-11-22 | 2018-05-31 | University Of Oslo | Albumin variants and uses thereof |
CN110770251A (zh) * | 2017-04-20 | 2020-02-07 | 诺和诺德股份有限公司 | 纯化白蛋白融合蛋白的方法 |
JP7282693B2 (ja) | 2017-06-20 | 2023-05-29 | アルブミディクス リミティド | 改良されたタンパク質発現株 |
CN112368368B (zh) * | 2018-06-15 | 2024-01-30 | 扶桑药品工业株式会社 | 辅助生殖医疗用培养基 |
US11369703B2 (en) | 2018-08-31 | 2022-06-28 | Genzyme Corporation | Sterile chromatography resin and use thereof in manufacturing processes |
CN111229023B (zh) * | 2018-11-29 | 2022-01-28 | 内蒙古东盛硅藻土科技创新产业园有限公司 | 一种化学降解添加剂 |
CN109879958A (zh) * | 2019-03-08 | 2019-06-14 | 中国人民解放军军事科学院军事医学研究院 | 一种低糖基化血清白蛋白的制备方法 |
US10501404B1 (en) | 2019-07-30 | 2019-12-10 | Factor Bioscience Inc. | Cationic lipids and transfection methods |
US20210096128A1 (en) * | 2019-10-01 | 2021-04-01 | Repligen Corporation | Determination of protein concentration in a fluid |
CN112858682B (zh) * | 2019-11-27 | 2023-06-02 | 广东唯实生物技术有限公司 | 用于尿微量白蛋白的检测试纸条及其制备方法、检测试剂盒和检测方法 |
WO2021111143A1 (en) | 2019-12-04 | 2021-06-10 | Albumedix Limited | Methods and compositions produced thereby |
US11739166B2 (en) | 2020-07-02 | 2023-08-29 | Davol Inc. | Reactive polysaccharide-based hemostatic agent |
CN112062833A (zh) * | 2020-10-09 | 2020-12-11 | 国药集团武汉血液制品有限公司 | 一种从血浆组分ⅳ沉淀中提取人血白蛋白的方法 |
CA3200066A1 (en) | 2020-12-08 | 2022-06-16 | Wei Xiang | Method for purifying recombinant protein |
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Family Cites Families (89)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
GB9019919D0 (en) | 1990-09-12 | 1990-10-24 | Delta Biotechnology Ltd | Purification of proteins |
US5625041A (en) * | 1990-09-12 | 1997-04-29 | Delta Biotechnology Limited | Purification of proteins |
US2433905A (en) * | 1943-11-01 | 1948-01-06 | Jr Walter L Hughes | Method for the crystallization of albumin and the preparation of protein products therefrom |
AT317418B (de) | 1972-06-16 | 1974-08-25 | Brigitte Panhofer | Verfahren zur Herstellung von intravenös beim Menschen anwendbarem Humanalbumin aus menschlichen Placenten |
FR2190437B1 (US07993877-20110809-P00003.png) * | 1972-07-05 | 1975-08-08 | Merieux Inst | |
CA1044537A (en) | 1973-05-09 | 1978-12-19 | Amf Incorporated | Filter medium and process |
DE2537123A1 (de) | 1975-08-20 | 1977-03-03 | New Zealand Inventions Dev | Verfahren zur herstellung von albumin |
SE405549B (sv) * | 1975-10-09 | 1978-12-18 | Pharmacia Fine Chemicals Ab | Forfarande for isolering av albumin ur plasmaprodukter genom kromatografisk fraktionering |
US4043997A (en) * | 1976-05-28 | 1977-08-23 | Cutter Laboratories, Inc. | Method for isolating albumin using insoluble supports coupled to a dye |
US4075197A (en) * | 1976-09-20 | 1978-02-21 | Monsanto Company | Serum albumin production |
US4269605A (en) | 1978-06-28 | 1981-05-26 | Amicon Corporation | Method and kit for separation of glycoproteins |
IN150740B (US07993877-20110809-P00003.png) * | 1978-11-24 | 1982-12-04 | Hoffmann La Roche | |
US4228154A (en) * | 1979-02-26 | 1980-10-14 | Armour Pharmaceutical Company | Purification of plasma albumin by ion exchange chromatography |
CA1149298A (en) | 1979-04-12 | 1983-07-05 | Eugene H. Wegner | Production of yeast cells at high cell densities |
US4222934A (en) * | 1979-04-12 | 1980-09-16 | American National Red Cross | Preparation of albumin using ethanol |
GB2053926B (en) | 1979-07-20 | 1983-02-23 | Atkinson A | Albumin extraction by affinity chromatography |
US4350156A (en) * | 1980-05-29 | 1982-09-21 | Japan Foundation For Artificial Organs | Method and apparatus for on-line filtration removal of macromolecules from a physiological fluid |
NZ199722A (en) | 1981-02-25 | 1985-12-13 | Genentech Inc | Dna transfer vector for expression of exogenous polypeptide in yeast;transformed yeast strain |
US4491946A (en) | 1981-03-09 | 1985-01-01 | Gould Inc. | Multi-station token pass communication system |
US4562251A (en) | 1981-03-26 | 1985-12-31 | Amicon Corporation | Agarose derivatives of amino phenyl boronic acid |
IL66614A (en) | 1981-08-28 | 1985-09-29 | Genentech Inc | Method of constructing a dna sequence encoding a polypeptide,microbial production of human serum albumin,and pharmaceutical compositions comprising it |
US4391801A (en) * | 1981-10-29 | 1983-07-05 | Cutter Laboratories, Inc. | Plasma protein fraction substantially free of acetate ions |
FR2543448A1 (fr) * | 1983-04-01 | 1984-10-05 | Rhone Poulenc Spec Chim | Procede de fractionnement du plasma |
US4748120A (en) * | 1983-05-02 | 1988-05-31 | Diamond Scientific Co. | Photochemical decontamination treatment of whole blood or blood components |
DE3344656A1 (de) | 1983-12-09 | 1985-06-13 | Lentia GmbH Chem. u. pharm. Erzeugnisse - Industriebedarf, 8000 München | Verfahren zur herstellung einer serumproteinloesung |
CA1286622C (en) | 1986-04-28 | 1991-07-23 | Chokyun Rha | Method for clarifying and stabilizing cell culture media |
JPS62294621A (ja) | 1986-06-13 | 1987-12-22 | Green Cross Corp:The | アルブミンの回収方法 |
JPS6383100A (ja) | 1986-09-26 | 1988-04-13 | Green Cross Corp:The | ヒト尿中アルブミンの製造方法 |
DE3888381T2 (de) | 1987-04-09 | 1994-07-28 | Delta Biotechnology Ltd | Hefevektor. |
US4833233A (en) | 1987-08-20 | 1989-05-23 | The United States Of America As Represented By The Administrator Of The National Aeronautics And Space Administration | Human serum albumin crystals and method of preparation |
CA1293217C (en) | 1987-11-09 | 1991-12-17 | Sooyoung Stanford Lee | Controlled growth rate fermentation |
IL88326A (en) | 1987-11-18 | 1993-03-15 | Gist Brocades Nv | Purification of serum albumin |
GB2214508A (en) | 1988-01-27 | 1989-09-06 | Bayer Ag | Plasmid vector for the efficient expression of foreign genes fused with newly conceived transcriptional and translational signal sequences. |
JPH01215289A (ja) | 1988-02-22 | 1989-08-29 | Toa Nenryo Kogyo Kk | 遺伝子組換えによる正常ヒト血清アルブミンaの製造方法 |
US4990447A (en) * | 1988-06-24 | 1991-02-05 | Gist-Brocades Nv | Process for the purification of serum albumin |
WO1990001063A1 (en) | 1988-07-23 | 1990-02-08 | Delta Biotechnology Limited | New secretory leader sequences |
FR2649991B2 (fr) | 1988-08-05 | 1994-03-04 | Rhone Poulenc Sante | Utilisation de derives stables du plasmide pkd1 pour l'expression et la secretion de proteines heterologues dans les levures du genre kluyveromyces |
US5277818A (en) * | 1988-10-31 | 1994-01-11 | The Green Cross Corporation | Albumin preparation and process for preparing the same |
JP3554796B2 (ja) | 1988-10-31 | 2004-08-18 | 三菱ウェルファーマ株式会社 | アルブミン製剤及びその製造方法 |
US4891221A (en) | 1988-11-23 | 1990-01-02 | Edward Shanborm | Whole blood antiviral process and composition |
FR2648048B1 (fr) | 1989-06-08 | 1994-06-03 | Lille Transfusion Sanguine | Procede de preparation de solutions d'albumine purifiee |
GB8913586D0 (en) | 1989-06-13 | 1989-08-02 | Technicol Limited | A method of determining the glycosylated protein level of a sample and an apparatus for use in the method |
JPH0768137B2 (ja) | 1989-06-15 | 1995-07-26 | 株式会社ミドリ十字 | アルブミン製剤及びその製法 |
SE500110C2 (sv) * | 1989-06-27 | 1994-04-18 | Kabi Pharmacia Ab | Sätt att rena ett protein från därtill bundna flervärda metalljoner |
GB8927480D0 (en) | 1989-12-05 | 1990-02-07 | Delta Biotechnology Ltd | Mutant fungal strain detection and new promoter |
JPH0671434B2 (ja) | 1989-09-18 | 1994-09-14 | 株式会社ミドリ十字 | ヒト血清アルブミンの製造方法 |
CA2022165C (en) | 1989-10-05 | 1999-11-23 | Chong E. Chang | Albumin purification |
US5250662A (en) * | 1989-10-05 | 1993-10-05 | Alpha Therapeutic Corporation | Albumin purification |
JP3127232B2 (ja) | 1990-03-08 | 2001-01-22 | ウェルファイド株式会社 | 蛋白質製剤の製造法 |
DE69133399T2 (de) | 1990-04-19 | 2005-06-30 | Bayer Corp. | Methode zur Herstellung von im Wesentlichen monomeren normalen menschlichen Serum-Albumin |
SE9002212D0 (sv) | 1990-06-21 | 1990-06-21 | Hightech Receptor Ab | Igg binding protein |
JP3230091B2 (ja) | 1990-06-25 | 2001-11-19 | ウェルファイド株式会社 | ヒト血清アルブミンの着色抑制方法 |
JP2982296B2 (ja) | 1990-11-19 | 1999-11-22 | 吉富製薬株式会社 | アルブミン含有水溶液の精製法 |
JP2949846B2 (ja) | 1990-11-30 | 1999-09-20 | 吉富製薬株式会社 | アルブミン製剤の保存方法 |
FR2672604B1 (fr) | 1991-02-07 | 1995-05-05 | Pasteur Merieux Serums Vacc | Procede pour isoler de l'albumine humaine a partir du surnageant iv, notamment iv-4, ou de la fraction v de cohn ou d'un surnageant ou fraction analogue. |
US5284777A (en) * | 1991-03-04 | 1994-02-08 | Isolab, Inc. | Combined glycated hemoglobin and immunoturbidometric glycated albumin assay from whole blood lysate |
JPH0671432B2 (ja) | 1991-03-20 | 1994-09-14 | 株式会社ミドリ十字 | ヒト血清アルブミンの製造方法 |
US5330901A (en) * | 1991-04-26 | 1994-07-19 | Research Corporation Technologies, Inc. | Expression of human serum albumin in Pichia pastoris |
DK0524681T3 (da) | 1991-07-12 | 2000-04-10 | Dsm Nv | Fremgangsmåde til oprensning af serumalbumin |
US5260308A (en) * | 1991-11-06 | 1993-11-09 | Mayo Foundation For Medical Education And Research | Method to increase permeability of the blood-nerve/brain barriers to proteins |
FR2686620B1 (fr) * | 1992-01-27 | 1995-06-23 | Rhone Poulenc Rorer Sa | Serum-albumine humaine, preparation et utilisation. |
US5281582A (en) | 1992-02-27 | 1994-01-25 | Alliance Pharmaceuticals, Corp. | Serum growth factor |
US5440018A (en) * | 1992-05-20 | 1995-08-08 | The Green Cross Corporation | Recombinant human serum albumin, process for producing the same and pharmaceutical preparation containing the same |
JPH07102148B2 (ja) * | 1992-05-20 | 1995-11-08 | 株式会社ミドリ十字 | 遺伝子操作により得られるヒト血清アルブミンの製造方法、およびそれにより得られるヒト血清アルブミン含有組成物 |
DE69309275T3 (de) * | 1992-06-24 | 2002-06-27 | Notetry Ltd., Little Somerford | Zyklonstaubsauger |
JP3360315B2 (ja) | 1992-07-31 | 2002-12-24 | 三菱ウェルファーマ株式会社 | ヒト血清アルブミンの高度精製方法 |
WO1994003636A1 (en) | 1992-08-03 | 1994-02-17 | Abbott Laboratories | Detecting and amplifying target nucleic acids using exonucleolytic activity |
DE4226971C2 (de) * | 1992-08-14 | 1997-01-16 | Widmar Prof Dr Tanner | Modifizierte Pilzzellen und Verfahren zur Herstellung rekombinanter Produkte |
US5728553A (en) * | 1992-09-23 | 1998-03-17 | Delta Biotechnology Limited | High purity albumin and method of producing |
CA2116385A1 (en) | 1993-02-25 | 1994-08-26 | Akinori Sumi | Human serum albumin and process for producing the same |
DE4308532A1 (de) | 1993-03-17 | 1994-09-22 | Boehringer Mannheim Gmbh | Monoklonale Antikörper gegen in vivo glykiertes Albumin |
SE9301583D0 (sv) * | 1993-05-07 | 1993-05-07 | Kabi Pharmacia Ab | Yeast strain and methods for expressing heterologous proteins in yeast |
CA2136564C (en) | 1993-11-26 | 2008-04-08 | Kaoru Kobayashi | Process for producing human serum albumin |
GB9404270D0 (en) | 1994-03-05 | 1994-04-20 | Delta Biotechnology Ltd | Yeast strains and modified albumins |
JPH07308199A (ja) | 1994-05-18 | 1995-11-28 | Green Cross Corp:The | ヒト血清アルブミンの製造方法 |
JP3702474B2 (ja) * | 1994-06-01 | 2005-10-05 | 三菱ウェルファーマ株式会社 | 血清アルブミン製剤の製造方法 |
GB9411356D0 (en) | 1994-06-07 | 1994-07-27 | Delta Biotechnology Ltd | Yeast strains |
GB2308006B (en) * | 1994-07-21 | 1998-07-22 | Gregory Lowell Millspaugh | Method of and system for controlling energy including in fusion |
US5561115A (en) | 1994-08-10 | 1996-10-01 | Bayer Corporation | Low temperature albumin fractionation using sodium caprylate as a partitioning agent |
DE69532492T2 (de) | 1994-08-31 | 2004-12-02 | Mitsubishi Pharma Corp. | Verfahren zur Reinigung von rekombinantem menschlichem Serumalbumin |
DE4432689A1 (de) | 1994-09-14 | 1996-03-21 | Basf Ag | Mischung aus Alkylierungsprodukten von acetalisierten Monosacchariden mit Epoxiden |
US6068995A (en) * | 1994-10-25 | 2000-05-30 | Yoshitomi Pharmaceutical Industries, Ltd. | Method for producing protein |
GB9526733D0 (en) | 1995-12-30 | 1996-02-28 | Delta Biotechnology Ltd | Fusion proteins |
AU4837996A (en) * | 1996-02-29 | 1997-09-16 | Delta Biotechnology Limited | High purity albumin production process |
GB9721892D0 (en) | 1997-10-15 | 1997-12-17 | British Tech Group | Apparatus for and method of testing a sample |
GB9902000D0 (en) * | 1999-01-30 | 1999-03-17 | Delta Biotechnology Ltd | Process |
JP4798832B2 (ja) | 2000-10-24 | 2011-10-19 | 一般財団法人化学及血清療法研究所 | ヒト血清アルブミン多量体の除去方法 |
US6693173B2 (en) | 2000-12-26 | 2004-02-17 | Alpha Therapeutic Corporation | Method to remove citrate and aluminum from proteins |
SE520854C2 (sv) | 2002-06-04 | 2003-09-02 | Wexioedisk Ab | Diskmaskin med uppsamlingsorgan för att ta emot diskvätska och sköljvätska |
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