WO2000044772A2 - Human serum albumin - Google Patents
Human serum albumin Download PDFInfo
- Publication number
- WO2000044772A2 WO2000044772A2 PCT/GB2000/000257 GB0000257W WO0044772A2 WO 2000044772 A2 WO2000044772 A2 WO 2000044772A2 GB 0000257 W GB0000257 W GB 0000257W WO 0044772 A2 WO0044772 A2 WO 0044772A2
- Authority
- WO
- WIPO (PCT)
- Prior art keywords
- albumin
- process according
- anion exchange
- cation exchange
- exchange chromatography
- Prior art date
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Classifications
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- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01D—SEPARATION
- B01D15/00—Separating processes involving the treatment of liquids with solid sorbents; Apparatus therefor
- B01D15/08—Selective adsorption, e.g. chromatography
- B01D15/26—Selective adsorption, e.g. chromatography characterised by the separation mechanism
- B01D15/38—Selective adsorption, e.g. chromatography characterised by the separation mechanism involving specific interaction not covered by one or more of groups B01D15/265 - B01D15/36
- B01D15/3804—Affinity chromatography
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
- A61P17/02—Drugs for dermatological disorders for treating wounds, ulcers, burns, scars, keloids, or the like
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P7/00—Drugs for disorders of the blood or the extracellular fluid
- A61P7/08—Plasma substitutes; Perfusion solutions; Dialytics or haemodialytics; Drugs for electrolytic or acid-base disorders, e.g. hypovolemic shock
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01D—SEPARATION
- B01D15/00—Separating processes involving the treatment of liquids with solid sorbents; Apparatus therefor
- B01D15/08—Selective adsorption, e.g. chromatography
- B01D15/26—Selective adsorption, e.g. chromatography characterised by the separation mechanism
- B01D15/36—Selective adsorption, e.g. chromatography characterised by the separation mechanism involving ionic interaction
- B01D15/361—Ion-exchange
- B01D15/362—Cation-exchange
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01D—SEPARATION
- B01D15/00—Separating processes involving the treatment of liquids with solid sorbents; Apparatus therefor
- B01D15/08—Selective adsorption, e.g. chromatography
- B01D15/26—Selective adsorption, e.g. chromatography characterised by the separation mechanism
- B01D15/36—Selective adsorption, e.g. chromatography characterised by the separation mechanism involving ionic interaction
- B01D15/361—Ion-exchange
- B01D15/363—Anion-exchange
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/14—Extraction; Separation; Purification
- C07K1/16—Extraction; Separation; Purification by chromatography
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/76—Albumins
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/76—Albumins
- C07K14/765—Serum albumin, e.g. HSA
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Analytical Chemistry (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Toxicology (AREA)
- Gastroenterology & Hepatology (AREA)
- Zoology (AREA)
- Public Health (AREA)
- General Chemical & Material Sciences (AREA)
- Veterinary Medicine (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Engineering & Computer Science (AREA)
- Animal Behavior & Ethology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Pharmacology & Pharmacy (AREA)
- Hematology (AREA)
- Dermatology (AREA)
- Diabetes (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Glass Compositions (AREA)
- Iron Core Of Rotating Electric Machines (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Treatment Of Liquids With Adsorbents In General (AREA)
Priority Applications (12)
Application Number | Priority Date | Filing Date | Title |
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CA2359705A CA2359705C (en) | 1999-01-30 | 2000-01-31 | Chromatographic process for purification of albumin |
JP2000596028A JP4586150B2 (ja) | 1999-01-30 | 2000-01-31 | 方法 |
DE60040967T DE60040967D1 (de) | 1999-01-30 | 2000-01-31 | Chromatographisches verfahren zur reinigung von albumin |
EP00901252A EP1149163B1 (en) | 1999-01-30 | 2000-01-31 | Chromatographic method for purification of albumin |
KR1020057009776A KR100886554B1 (ko) | 1999-01-30 | 2000-01-31 | 알부민 용액의 정제방법 |
AU21207/00A AU763899B2 (en) | 1999-01-30 | 2000-01-31 | Process |
MXPA01007719A MXPA01007719A (es) | 1999-01-30 | 2000-01-31 | Procedimiento. |
HK02104220.2A HK1042521B (zh) | 1999-01-30 | 2002-06-04 | 生產重組白蛋白的方法 |
AU2003248302A AU2003248302B2 (en) | 1999-01-30 | 2003-09-23 | Process |
US12/207,325 US7993877B2 (en) | 1999-01-30 | 2008-09-09 | Process for the purification of recombinant albumin |
US13/175,155 US9029102B2 (en) | 1999-01-30 | 2011-07-01 | Process for the purification of recombinant albumin |
US14/330,703 US9555344B2 (en) | 1999-01-30 | 2014-07-14 | Process for the purification of recombinant albumin |
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
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GB9902000A GB9902000D0 (en) | 1999-01-30 | 1999-01-30 | Process |
GB9902000.0 | 1999-01-30 |
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US09890297 A-371-Of-International | 2000-01-31 | ||
US12/207,325 Continuation US7993877B2 (en) | 1999-01-30 | 2008-09-09 | Process for the purification of recombinant albumin |
Publications (2)
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WO2000044772A2 true WO2000044772A2 (en) | 2000-08-03 |
WO2000044772A3 WO2000044772A3 (en) | 2000-11-30 |
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Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
PCT/GB2000/000257 WO2000044772A2 (en) | 1999-01-30 | 2000-01-31 | Human serum albumin |
Country Status (16)
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US11241505B2 (en) | 2015-02-13 | 2022-02-08 | Factor Bioscience Inc. | Nucleic acid products and methods of administration thereof |
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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 |
CA3033788A1 (en) | 2016-08-17 | 2018-02-22 | Factor Bioscience Inc. | Nucleic acid products and methods of administration thereof |
WO2020046602A1 (en) | 2018-08-31 | 2020-03-05 | Genzyme Corporation | Sterile chromatography resin and use thereof in manufacturing processes |
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US10501404B1 (en) | 2019-07-30 | 2019-12-10 | Factor Bioscience Inc. | Cationic lipids and transfection methods |
EP4038349A4 (en) * | 2019-10-01 | 2022-12-28 | Repligen Corporation | DETERMINATION OF THE PROTEIN CONCENTRATION OF A FLUID |
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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 |
CN114885608A (zh) | 2020-12-08 | 2022-08-09 | 通化安睿特生物制药股份有限公司 | 纯化重组蛋白的方法 |
CN112646045A (zh) * | 2021-01-06 | 2021-04-13 | 海默斯(重庆)医学生物技术有限公司 | 一种重组角蛋白分离纯化方法 |
CN114907469A (zh) * | 2021-02-08 | 2022-08-16 | 首都医科大学附属北京朝阳医院 | 一种人血清中白蛋白分离纯化方法 |
CN113735963A (zh) * | 2021-09-10 | 2021-12-03 | 山东健通生物科技有限公司 | 一种重组人血清白蛋白纯化过程去除色素的方法 |
Citations (5)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO1991000290A1 (en) * | 1989-06-27 | 1991-01-10 | Kabi Pharmacia Ab | Method of cleansing proteins |
US5284777A (en) * | 1991-03-04 | 1994-02-08 | Isolab, Inc. | Combined glycated hemoglobin and immunoturbidometric glycated albumin assay from whole blood lysate |
WO1994004687A1 (en) * | 1992-08-14 | 1994-03-03 | Rhone-Poulenc Rorer S.A. | Modified fungal cells and method for producing recombinant products |
WO1994026873A1 (en) * | 1993-05-07 | 1994-11-24 | Pharmacia Ab | Yeast strain and methods for expressing heterologous proteins in yeast |
WO1997031947A1 (en) * | 1996-02-29 | 1997-09-04 | Delta Biotechnology Limited | High purity albumin production process |
Family Cites Families (84)
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 |
WO1988008027A1 (en) | 1987-04-09 | 1988-10-20 | Delta Biotechnology Limited | Yeast vector |
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 |
JP3092811B2 (ja) | 1988-07-23 | 2000-09-25 | デルタ バイオテクノロジー リミテッド | ペプチドおよびdna配列 |
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 |
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 |
US5277818A (en) * | 1988-10-31 | 1994-01-11 | The Green Cross Corporation | Albumin preparation and process for preparing the same |
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 |
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 |
EP0452753B1 (en) | 1990-04-19 | 2004-06-23 | Bayer Corporation | Method for preparing essentially monomeric normal serum albumin (human) |
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. |
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 |
WO1993001207A1 (en) | 1991-07-12 | 1993-01-21 | Gist-Brocades N.V. | Process for the purification of serum albumin |
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 |
SG46302A1 (en) * | 1992-06-24 | 1998-02-20 | Notetry Ltd | Vacuum cleaner |
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 |
DE69329824T2 (de) | 1992-08-03 | 2001-08-09 | Abbott Lab | Nachweis und amplifikation bestimmter nukleinsäuren mittels exonukleolytischer aktivität |
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 |
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 |
WO1996003751A1 (en) * | 1994-07-21 | 1996-02-08 | Gregory Lowell Millspaugh | Method of and system for controlling energy, including in fusion reactors |
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 |
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 |
SE0201680L (sv) | 2002-06-04 | 2003-09-02 | Wexioedisk Ab | Diskmaskin med uppsamlingsorgan för att ta emot diskvätska och sköljvätska |
-
1999
- 1999-01-30 GB GB9902000A patent/GB9902000D0/en not_active Ceased
-
2000
- 2000-01-31 CN CN2005101086585A patent/CN1810834B/zh not_active Expired - Lifetime
- 2000-01-31 KR KR1020017009551A patent/KR100577493B1/ko active IP Right Grant
- 2000-01-31 EP EP20100075421 patent/EP2272961A1/en not_active Withdrawn
- 2000-01-31 CN CNA2006101006640A patent/CN1974599A/zh active Pending
- 2000-01-31 CN CNB008032920A patent/CN1211485C/zh not_active Expired - Lifetime
- 2000-01-31 JP JP2000596028A patent/JP4586150B2/ja not_active Expired - Lifetime
- 2000-01-31 EP EP00901252A patent/EP1149163B1/en not_active Expired - Lifetime
- 2000-01-31 SG SG2007061591A patent/SG174629A1/en unknown
- 2000-01-31 CA CA2359705A patent/CA2359705C/en not_active Expired - Lifetime
- 2000-01-31 EP EP20080166355 patent/EP2048234B1/en not_active Expired - Lifetime
- 2000-01-31 SG SG200304297A patent/SG119194A1/en unknown
- 2000-01-31 DK DK08166355T patent/DK2048234T3/da active
- 2000-01-31 MX MXPA01007719A patent/MXPA01007719A/es active IP Right Grant
- 2000-01-31 AU AU21207/00A patent/AU763899B2/en not_active Expired
- 2000-01-31 KR KR1020057009776A patent/KR100886554B1/ko active IP Right Grant
- 2000-01-31 CN CN2004100050153A patent/CN1526732B/zh not_active Expired - Lifetime
- 2000-01-31 WO PCT/GB2000/000257 patent/WO2000044772A2/en active IP Right Grant
- 2000-01-31 AT AT00901252T patent/ATE416254T1/de not_active IP Right Cessation
- 2000-01-31 DE DE60040967T patent/DE60040967D1/de not_active Expired - Lifetime
- 2000-01-31 ES ES00901252T patent/ES2317827T3/es not_active Expired - Lifetime
-
2002
- 2002-06-04 HK HK07101272A patent/HK1096691A1/xx not_active IP Right Cessation
- 2002-06-04 HK HK02104220.2A patent/HK1042521B/zh unknown
-
2003
- 2003-09-23 AU AU2003248302A patent/AU2003248302B2/en not_active Expired
-
2008
- 2008-09-09 US US12/207,325 patent/US7993877B2/en not_active Expired - Fee Related
-
2010
- 2010-05-27 JP JP2010121914A patent/JP5474661B2/ja not_active Expired - Lifetime
-
2011
- 2011-07-01 US US13/175,155 patent/US9029102B2/en not_active Expired - Fee Related
-
2013
- 2013-01-15 JP JP2013004867A patent/JP5774612B2/ja not_active Expired - Lifetime
-
2014
- 2014-07-14 US US14/330,703 patent/US9555344B2/en not_active Expired - Fee Related
Patent Citations (5)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO1991000290A1 (en) * | 1989-06-27 | 1991-01-10 | Kabi Pharmacia Ab | Method of cleansing proteins |
US5284777A (en) * | 1991-03-04 | 1994-02-08 | Isolab, Inc. | Combined glycated hemoglobin and immunoturbidometric glycated albumin assay from whole blood lysate |
WO1994004687A1 (en) * | 1992-08-14 | 1994-03-03 | Rhone-Poulenc Rorer S.A. | Modified fungal cells and method for producing recombinant products |
WO1994026873A1 (en) * | 1993-05-07 | 1994-11-24 | Pharmacia Ab | Yeast strain and methods for expressing heterologous proteins in yeast |
WO1997031947A1 (en) * | 1996-02-29 | 1997-09-04 | Delta Biotechnology Limited | High purity albumin production process |
Non-Patent Citations (4)
Title |
---|
GOWARD, C. R. ET AL.: "Expression and purification of a truncated recombinant streptococcal protein." BIOCHEM. J. , vol. 267, 1990, pages 171-177, XP002045030 * |
REISS, A.L. ET AL.: "The Efficacy of Chelating Agents in Removing Nickel from Human Albumin in Vitro." NICKEL TOXICOL., PROC. INT. CONF., 2ND, 1980, pages 91-94, XP000933887 * |
SARKAR, B.: "Bioinorganic Chemistry of Nickel" NATO ADV. STUDY INST. SER., SER. C, BIOENERG. THERMODYN.: MODEL SYST., vol. 55, 1980, pages 23-32, XP000933817 * |
See also references of EP1149163A2 * |
Cited By (122)
Publication number | Priority date | Publication date | Assignee | Title |
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EP2216409A1 (en) | 2000-04-12 | 2010-08-11 | Human Genome Sciences, Inc. | Albumin fusion proteins |
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GB2424888B (en) * | 2003-12-23 | 2008-03-26 | Delta Biotechnology Ltd | 2-Micron family plasmid and use thereof |
US8252551B2 (en) | 2003-12-23 | 2012-08-28 | Novozymes Biopharma Dk A/S | 2-micron family plasmid and use thereof |
GB2424888A (en) * | 2003-12-23 | 2006-10-11 | Delta Biotechnology Ltd | 2-Micron family plasmid and use thereof |
EP2169067A1 (en) * | 2004-12-22 | 2010-03-31 | Novozymes A/S | Recombinant production of serum albumin |
WO2006066595A3 (en) * | 2004-12-22 | 2006-08-31 | Novozymes As | Recombinant production of serum albumin |
WO2006066595A2 (en) * | 2004-12-22 | 2006-06-29 | Novozymes A/S | Recombinant production of serum albumin |
EP2330200A2 (en) | 2004-12-23 | 2011-06-08 | Novozymes Biopharma DK A/S | Gene expression technique |
WO2006067511A1 (en) | 2004-12-23 | 2006-06-29 | Novozymes Delta Limited | Gene expression technique |
WO2007063129A3 (en) * | 2005-12-02 | 2007-07-12 | Novozymes As | Insolation of peptides , polypeptides and proteins |
WO2007063129A2 (en) * | 2005-12-02 | 2007-06-07 | Novozymes A/S | Insolation of peptides , polypeptides and proteins |
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 |
US9505823B2 (en) | 2006-08-07 | 2016-11-29 | TEV A Biopharmaceuticals USA, Inc. | Albumin-insulin fusion proteins |
EP2594583A1 (en) | 2007-08-08 | 2013-05-22 | Novozymes Biopharma DK A/S | Transferrin variants and conugates |
EP2604623A2 (en) | 2007-08-08 | 2013-06-19 | Novozymes Biopharma DK A/S | Transferrin variants and conjugates |
WO2009019314A1 (en) | 2007-08-08 | 2009-02-12 | Novozymes A/S | Transferrin variants and conjugates |
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 |
WO2010066090A1 (zh) | 2008-12-10 | 2010-06-17 | 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 |
US11555061B2 (en) | 2009-02-11 | 2023-01-17 | Albumedix, Ltd | Albumin variants and conjugates |
EP3243835A1 (en) | 2009-02-11 | 2017-11-15 | Albumedix A/S | Albumin variants and conjugates |
US9493545B2 (en) | 2009-02-11 | 2016-11-15 | Albumedix A/S | Albumin variants and conjugates |
WO2010092135A2 (en) | 2009-02-11 | 2010-08-19 | Novozymes Biopharma Uk Ltd. | Albumin variants and conjugates |
US11492389B1 (en) | 2009-02-20 | 2022-11-08 | Ventria Biosciences Inc. | Cell culture media containing combinations of proteins |
WO2010115634A1 (en) | 2009-04-09 | 2010-10-14 | Cellca Gmbh | Method for improved single cell cloning |
CN102549012A (zh) * | 2009-05-07 | 2012-07-04 | 诺维信生物制药丹麦公司 | 纯化白蛋白的方法 |
WO2010128143A1 (en) | 2009-05-07 | 2010-11-11 | Novozymes Biopharma Dk A/S | Method of controlling o-linked glycosylation of antibodies |
US9403898B2 (en) | 2009-05-07 | 2016-08-02 | Novozymes Biopharma Dk A/S | Method for purifying albumin |
WO2010128142A1 (en) * | 2009-05-07 | 2010-11-11 | Novozymes Biopharma Dk A/S | Method for purifying albumin |
CN102549012B (zh) * | 2009-05-07 | 2015-07-01 | 诺维信生物制药丹麦公司 | 纯化白蛋白的方法 |
US11530400B2 (en) | 2009-07-13 | 2022-12-20 | Allergan, Inc. | Process and system for obtaining botulinum neurotoxin |
US11124786B2 (en) | 2009-07-13 | 2021-09-21 | Allergan, Inc. | Process and system for obtaining botulinum neurotoxin |
US11518986B2 (en) | 2009-07-13 | 2022-12-06 | Allergan, Inc. | Process and system for obtaining botulinum neurotoxin |
US11203748B2 (en) | 2009-07-13 | 2021-12-21 | Allergan, Inc. | Process and system for obtaining botulinum neurotoxin |
US11326155B2 (en) | 2009-07-13 | 2022-05-10 | Allergan, Inc. | Process and system for obtaining botulinum neurotoxin |
US11525130B2 (en) | 2009-07-13 | 2022-12-13 | Allergan, Inc. | Process and system for obtaining botulinum neurotoxin |
EP3173094A1 (en) | 2009-10-26 | 2017-05-31 | General Regeneratives (shanghai) limited | Use of interleukin-1 receptor antagonist for preparing medicament for preventing or treating epithelium trauma of intestinal mucosa |
US10696732B2 (en) | 2009-10-30 | 2020-06-30 | Albumedix, Ltd | Albumin variants |
US8748380B2 (en) | 2009-10-30 | 2014-06-10 | Novozymes Biopharma Dk A/S | Albumin variants |
EP3421491A2 (en) | 2009-10-30 | 2019-01-02 | Albumedix Ltd | Albumin variants |
WO2011051489A2 (en) | 2009-10-30 | 2011-05-05 | Novozymes Biopharma Dk A/S | Albumin variants |
US10233228B2 (en) | 2010-04-09 | 2019-03-19 | Albumedix Ltd | Albumin derivatives and variants |
WO2011124718A1 (en) | 2010-04-09 | 2011-10-13 | Novozymes A/S | Albumin derivatives and variants |
CN103025757A (zh) * | 2010-04-29 | 2013-04-03 | 巴克斯特国际有限公司 | 二价阳离子结合蛋白在阴离子交换树脂上的纯化方法 |
WO2012059486A1 (en) | 2010-11-01 | 2012-05-10 | Novozymes Biopharma Dk A/S | Albumin variants |
US10183984B2 (en) | 2010-12-20 | 2019-01-22 | Healthgen Biotechnology Corp. | Method for extracting recombinant human serum albumin from transgenic rice grain |
US9255138B2 (en) | 2010-12-20 | 2016-02-09 | Healthgen Biotechnology Co., Ltd. | Method for extracting recombinant human serum albumin from transgenic rice grain |
KR101830803B1 (ko) * | 2010-12-20 | 2018-02-21 | 우한 헬스젠 바이오테크놀로지 코포레이션 | 형질전환 쌀 알곡으로부터 인간 혈청 알부민을 추출하는 방법 |
EP2655397A1 (en) * | 2010-12-20 | 2013-10-30 | Healthgen Biotechnology Co., Ltd. | Method for extracting human serum albumin from transgenic rice grain |
EP2655397A4 (en) * | 2010-12-20 | 2015-01-21 | Healthgen Biotechnology Co Ltd | PROCESS FOR EXTRACTING HUMAN ALUMUM SERUM FROM TRANSGENIC RICE GRAIN |
WO2012083580A1 (en) | 2010-12-24 | 2012-06-28 | Healthgen Biotechnology Co., Ltd. | Method for purifying human serum albumin from transgenic rice grain |
US9951100B2 (en) | 2010-12-24 | 2018-04-24 | Healthgen Biotechnology Co., Ltd. | Method for isolating and purifying recombinant human serum albumin from transgenic rice grain |
US9023990B2 (en) | 2010-12-24 | 2015-05-05 | Healthgen Biotechnology Co., Ltd. | Method for isolating and purifying recombinant human serum albumin from transgenic rice grain |
US10428107B2 (en) | 2010-12-24 | 2019-10-01 | Healthgen Biotechnology Co., Ltd. | Method for isolating and purifying recombinant human serum albumin from transgenic rice grain |
US8822417B2 (en) | 2011-05-05 | 2014-09-02 | Novozymes Biopharma DIC A/S | Albumin variants |
WO2013006675A1 (en) | 2011-07-05 | 2013-01-10 | Novozymes Biopharma Uk Limited | Albumin formulation and use |
US10844349B2 (en) | 2011-07-05 | 2020-11-24 | Albumedix Ltd. | Albumin formulation and use |
EP2729492B1 (en) * | 2011-07-05 | 2019-01-02 | Albumedix Ltd | Albumin formulation and use |
US10711050B2 (en) | 2011-11-18 | 2020-07-14 | Albumedix Ltd | Variant serum albumin with improved half-life and other properties |
KR102196339B1 (ko) | 2011-12-05 | 2020-12-29 | 팩터 바이오사이언스 인크. | 세포를 형질감염시키는 방법들 및 생성물들 |
KR20140109925A (ko) * | 2011-12-05 | 2014-09-16 | 팩터 바이오사이언스 인크. | 세포를 형질감염시키는 방법들 및 생성물들 |
KR102320571B1 (ko) | 2011-12-05 | 2021-11-02 | 팩터 바이오사이언스 인크. | 세포를 형질감염시키는 방법들 및 생성물들 |
US11692203B2 (en) | 2011-12-05 | 2023-07-04 | Factor Bioscience Inc. | Methods and products for transfecting cells |
US11708586B2 (en) | 2011-12-05 | 2023-07-25 | Factor Bioscience Inc. | Methods and products for transfecting cells |
EP2788033A4 (en) * | 2011-12-05 | 2015-08-26 | Factor Bioscience Inc | METHODS AND PRODUCTS FOR THE TRANSFECTION OF CELLS |
KR20210005287A (ko) * | 2011-12-05 | 2021-01-13 | 팩터 바이오사이언스 인크. | 세포를 형질감염시키는 방법들 및 생성물들 |
US10329340B2 (en) | 2012-03-16 | 2019-06-25 | Albumedix Ltd | Albumin variants |
US9944691B2 (en) | 2012-03-16 | 2018-04-17 | Albumedix A/S | Albumin variants |
WO2013135896A1 (en) | 2012-03-16 | 2013-09-19 | Novozymes Biopharma Dk A/S | Albumin variants |
US10934341B2 (en) | 2012-11-08 | 2021-03-02 | Albumedix, Ltd. | Albumin variants |
US10501524B2 (en) | 2012-11-08 | 2019-12-10 | Albumedix Ltd | Albumin variants |
US10730926B2 (en) | 2012-12-21 | 2020-08-04 | Wuhan Healthgen Biotechnology Corp | Chromatographic method for isolating and purifying high-purity recombined human serum albumin |
WO2014094406A1 (zh) | 2012-12-21 | 2014-06-26 | 武汉禾元生物科技有限公司 | 一种分离纯化高纯度重组人血清白蛋白的层析方法 |
EP3398964A1 (en) | 2012-12-21 | 2018-11-07 | Wuhan Healthgen Biotechnology Corp | Chromatographic method for isolating and purifying high-purity recombined human serum albumin |
JP2016514957A (ja) * | 2013-03-06 | 2016-05-26 | グラクソスミスクライン・リミテッド・ライアビリティ・カンパニーGlaxoSmithKline LLC | 宿主細胞および使用方法 |
JP2019122395A (ja) * | 2013-03-06 | 2019-07-25 | グラクソスミスクライン・リミテッド・ライアビリティ・カンパニーGlaxoSmithKline LLC | 宿主細胞および使用方法 |
WO2015063611A2 (en) | 2013-11-01 | 2015-05-07 | University Of Oslo | Albumin variants and uses thereof |
WO2016207730A1 (en) | 2015-06-22 | 2016-12-29 | The University Of Oslo | Targeting of vaccine antigen to an intracellular compartment |
US10633428B2 (en) | 2015-08-20 | 2020-04-28 | Albumedix Ltd | Albumin variants and conjugates |
US10023618B2 (en) | 2015-12-22 | 2018-07-17 | Albumedix A/S | Protein expression strains |
WO2017112847A1 (en) | 2015-12-22 | 2017-06-29 | Albumedix A/S | Improved protein expression strains |
EP3603391A1 (en) | 2016-10-04 | 2020-02-05 | Albumedix Ltd | Uses of recombinant yeast-derived serum albumin |
WO2018065491A1 (en) | 2016-10-04 | 2018-04-12 | Albumedix A/S | Uses of recombinant yeast-derived serum albumin |
WO2018096396A1 (en) | 2016-11-22 | 2018-05-31 | University Of Oslo | Albumin variants and uses thereof |
WO2018193033A1 (en) * | 2017-04-20 | 2018-10-25 | Novo Nordisk A/S | Methods of purification of albumin fusion proteins |
US11396670B2 (en) | 2017-06-20 | 2022-07-26 | Albumedix Limited | Protein expression strains |
US11130979B2 (en) | 2017-06-20 | 2021-09-28 | Albumedix Ltd | Protein expression strains |
EP3808837A4 (en) * | 2018-06-15 | 2022-04-06 | Fuso Pharmaceutical Industries, Ltd. | CULTURE MEDIA FOR ASSISTED REPRODUCTIVE TECHNOLOGY |
JPWO2019240255A1 (ja) * | 2018-06-15 | 2021-07-15 | 扶桑薬品工業株式会社 | 生殖補助医療用培地 |
CN112368368A (zh) * | 2018-06-15 | 2021-02-12 | 扶桑药品工业株式会社 | 辅助生殖医疗用培养基 |
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 |
WO2021111143A1 (en) | 2019-12-04 | 2021-06-10 | Albumedix Limited | Methods and compositions produced thereby |
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