WO1990015617A1 - Albumin preparation and method of producing the same - Google Patents
Albumin preparation and method of producing the same Download PDFInfo
- Publication number
- WO1990015617A1 WO1990015617A1 PCT/JP1990/000788 JP9000788W WO9015617A1 WO 1990015617 A1 WO1990015617 A1 WO 1990015617A1 JP 9000788 W JP9000788 W JP 9000788W WO 9015617 A1 WO9015617 A1 WO 9015617A1
- Authority
- WO
- WIPO (PCT)
- Prior art keywords
- albumin
- preparation
- exchanger
- albumin preparation
- anion exchanger
- Prior art date
Links
Classifications
-
- 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
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61L—METHODS OR APPARATUS FOR STERILISING MATERIALS OR OBJECTS IN GENERAL; DISINFECTION, STERILISATION OR DEODORISATION OF AIR; CHEMICAL ASPECTS OF BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES; MATERIALS FOR BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES
- A61L2/00—Methods or apparatus for disinfecting or sterilising materials or objects other than foodstuffs or contact lenses; Accessories therefor
- A61L2/0005—Methods or apparatus for disinfecting or sterilising materials or objects other than foodstuffs or contact lenses; Accessories therefor for pharmaceuticals, biologicals or living parts
- A61L2/0011—Methods or apparatus for disinfecting or sterilising materials or objects other than foodstuffs or contact lenses; Accessories therefor for pharmaceuticals, biologicals or living parts using physical methods
- A61L2/0023—Heat
-
- 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
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Definitions
- the present invention relates to an albumin preparation and a method for producing the same. More specifically, the present invention relates to a serum albumin preparation having reduced aggregate content, contaminant protein content, and the like, and a method for producing the same.
- Serum albumin is the most abundant protein in plasma, and functions in blood to maintain osmotic pressure and to bind nutrients and metabolites to transport them.
- the above-mentioned preparations containing serum albumin are used for treatment of hypoalbuminemia, hemorrhagic shock, etc. due to albumin loss and reduced albumin synthesis.
- heat treatment in the form of an albumin-containing aqueous solution is generally used to inactivate viruses that may be contaminated there.
- a commercially available albumin preparation produced by such a method is analyzed by gel filtration analysis, it is known that aggregates are present in the preparation.
- this aggregate (generally referred to as a polymer, hereinafter referred to as a polymer) hardly exists before the above heat treatment, the heat treatment causes heat-stable contaminant proteins to aggregate the albumin. Probably. Since commercially available albumin preparations are widely used safely, this polymer is not considered to be particularly harmful to humans.However, since it is a heat-modified product, it should be contained as little as possible in the preparation. I like it.
- albumin such as transferrin is contained in albumin. It contains contaminating proteins that are relatively similar in physical and chemical properties to Bumin, and it is difficult to separate efficiently using conventional means such as fractionation. There is a problem that remains.
- an object of the present invention is to provide an albumin preparation having a low polymer content and a low content of contaminating proteins, and a method for producing the same.
- the albumin preparation of the present invention which has been made to solve the above-mentioned problems, is characterized in that the polymer content measured by gel filtration analysis is below the detection limit, and the Mancini method was used. It is a preparation characterized by the fact that the transferrin content is below the detection limit.
- the method for producing an albumin preparation of the present invention is characterized in that an aqueous solution containing serum albumin is treated with an anion exchanger, then treated with a cation exchanger, and then heated.
- a strong anion exchanger and a strong cation exchanger are preferable as the anion exchanger and the cation exchanger used for treating the albumin aqueous solution, respectively.
- albumin which is the main component of the preparation of the present invention and the starting material for the production method of the present invention.
- mammals such as humans, magpies, and egrets, Origin In particular, those derived from human are used.
- the starting material for preparing albumin include Fraction V obtained by the cold alcohol fractionation of Mr. Kohn.
- the albumin preparation of the present invention can be obtained by treating an albumin-containing aqueous solution obtained by dissolving the above-mentioned serum albumin in appropriate purified water, treating with an anion exchanger, treating with a cation exchanger, and then heating.
- an albumin-containing aqueous solution obtained by dissolving the above-mentioned serum albumin in appropriate purified water, treating with an anion exchanger, treating with a cation exchanger, and then heating.
- the albumin content in the aqueous solution containing albumin is usually adjusted to about 0.1 to 30% (WXV; the same applies hereinafter unless otherwise specified), and preferably about 1 to 10%. You.
- an albumin aqueous solution is first subjected to an anion exchanger treatment for purification.
- anion exchanger treatment contaminant proteins having a lower isoelectric point than albumin, such as habutoglobin,,-acidic glycoprotein, are removed and purified.
- any inert carrier having an anion exchange group for example, getylaminoethyl group, etc. can be used.
- anion exchangers such as DEAE-Sepharose®, Q—Sepharose II (both from Pharmacia), DEAE—Toyopearl®, QAE-Toyopar ⁇ ), A200 cell mouth fin ® (manufactured by Seikagaku Corporation), anion exchange resin and the like.
- strong anion exchangers such as Q-Sepharose, QAE-Toyopearl It is preferable to use it.
- the above treatment using an anion exchanger is performed by bringing an aqueous albumin solution into contact with an anion exchanger.
- the amount of the anion exchanger used is appropriately adjusted depending on the contaminant protein content in the aqueous solution containing albumin, the exchange capacity of the anion exchanger, etc., and the anion exchanger is 0.1 to 5 per gram of albumin, usually about 3 used.
- This method may be performed by either the dynamic ram method or the batch method, but is preferably performed by the column method in view of the efficiency of removing contaminating proteins.
- the albumin aqueous solution is adjusted to a pH of about 3 to 6, preferably 114.5 to 5.5, and a salt concentration of about 0.001 to 0.2M sodium chloride, preferably Adjusted to 0.001 to 0.05M, passed through an anion exchanger ram equilibrated with a buffer solution (for example, 0.02M sodium acetate (pH 5.1)), and then developed with the same buffer solution. This is performed by recovering the non-adsorbed components.
- the above operation is preferably performed at a low temperature (usually 10 ° C. or lower) in order to suppress denaturation of albumin.
- an anion exchanger is added to and brought into contact with the aqueous albumin solution adjusted to the above conditions, mixed at 10 ° C or less, for 30 minutes to 2 hours, and then centrifuged. This is performed by separating from the anion exchanger by means of (1) and collecting the supernatant.
- the aqueous albumin solution purified by the above-described anion exchanger treatment is subjected to a cation exchanger treatment after further pH adjustment, concentration adjustment and the like, if necessary.
- contaminant proteins such as transferrin having an isoelectric point at a higher pH than that of albumin or the like are removed and purified.
- any insoluble carrier having a cation exchange group for example, sulfo group, carboxyl group, etc.
- cation exchangers commonly used in this field such as SP-Sephadex® (Pharmacia), SP-Toyopearl®, TSKgelSP-5PW® (all And a strong cation exchanger such as SP-Sepharose and SP-Toyopearl from the viewpoint of the efficiency of removing contaminating proteins.
- the treatment using the cation exchanger is carried out by bringing the aqueous albumin solution purified by the anion exchanger treatment into contact with the cation exchanger.
- the amount of the cation exchanger used is appropriately adjusted depending on the contaminant protein content in the aqueous albumin solution, the exchange capacity of the cation exchanger, etc., and the cation exchanger is 0.1 to 5 ⁇ per gram of albumin, usually 2 ? ⁇ Used around.
- This method may be performed by either the column method or the batch method, but is preferably performed by the force-ram method in view of the efficiency of removing contaminating proteins.
- the above-mentioned aqueous albumin solution is used in a concentration of about ⁇ 4 to 8, preferably ⁇ 4.5 to 6.0, more preferably ⁇ 5.5, and a salt concentration of about 0.001 to 0.2% sodium chloride.
- the pH is adjusted to 0.001 to 0.05 ⁇ , and the buffer [e.g., 0.021 V [sodium acetate
- the above operation is preferably performed at a low temperature (usually 10 or less) in order to suppress denaturation of albumin.
- a cation exchanger is added to and brought into contact with the aqueous albumin solution adjusted to the above conditions, mixed at 10 ° C or lower, for 30 minutes to 2 hours, and then centrifuged. By means of It is performed by separating from the ion exchanger and collecting the supernatant.
- the amount of contaminating proteins contained in the aqueous albumin solution purified by the anion exchanger treatment and the cation exchanger treatment is less than the detection limit of haptoglobin, transinsulin and monoacid glycoprotein.
- the aqueous albumin solution in which the content of contaminating proteins has been reduced by the above-described anion exchanger treatment and cation exchanger treatment is adjusted to an appropriate concentration, and is formulated into a desired formulation such as filling a vial.
- heat treatment is performed to obtain an albumin preparation of the present invention.
- the above heat treatment inactivates viruses that may be mixed into the albumin preparation, and is performed as an aqueous solution adjusted to an albumin concentration of about 5 to 30%, usually about 5 or 20 to 25%.
- the temperature may be a temperature and time sufficient to inactivate contaminating viruses, and is, for example, 50 to 70, preferably about 60, for 5 to 20 hours, and preferably about 10 hours.
- an albumin stabilizer for example, sodium N-acetyltributanofanate, sodium caprylate, or the like may be added alone or as a mixture, if necessary. Good. These albumin stabilizers are used in an amount of 20 to 60 mg, preferably about 40 mg, per 1 g of albumin contained in the preparation.
- the polymer content measured by gel filtration analysis is below the detection limit
- the transphenylene content measured by the Mancini method is below the detection limit
- the albumin preparation of the present invention is used in the same dosage and usage as the conventional albumin preparation.
- FIG. 1 to FIG. 3 are graphs showing standard curves by a one-way immunodiffusion method for —acid glycoprotein, hubby globin, and transferrin, respectively.
- Fraction V (1.5 g) obtained by Mr. Kohn's cold alcohol fractionation was dissolved in cold sterile distilled water 2.0 ⁇ , and the pH was adjusted to 4.6 with acetic acid. Stir for 1 hour. Then, the mixture was filtered at about 12 ° C (filter: 0.45 liters), further added with cold sterile distilled water 2. O, adjusted to pH 5.1 with 1N sodium hydroxide, and added to an aqueous albumin solution. I got
- aqueous albumin solution obtained in the above (3) was added 1.2 ⁇ of a stabilizer solution per aqueous solution (containing 5.55 g of N-acetyltributophane and 3.89 g of sodium sodium perrylate in 100 ⁇ ), After adjusting the pH to 6.85 with IN sodium hydroxide, the bacteria were filtered off. Next, after adjusting the albumin concentration to 25%, a predetermined amount was dispensed into vials and heat-treated at 60 ° C for 10 hours to obtain an albumin preparation.
- a stabilizer solution per aqueous solution containing 5.55 g of N-acetyltributophane and 3.89 g of sodium sodium perrylate in 100 ⁇
- the polymer content of the obtained preparation of the present invention was measured by gel filtration analysis, no polymer was detected.
- the polymer content of an albumin preparation (hereinafter referred to as comparative preparation) prepared in substantially the same manner as the above-mentioned production method except that the SP-Toyopearl column treatment step was omitted, was compared to the albumin content.
- the gel filtration analysis was performed under the following conditions.
- Sample A solution obtained by diluting the preparation of the present invention and the comparative preparation 50-fold with the following buffer and filtering (filter: 0.45 lord) Injected.
- the albumin preparation of the present invention was prepared by using the! -AG. Both Hp and ⁇ were below the detection limit and were found to be extremely low in contaminant protein content. As is evident from Figs. 1 to 3, the detection limit of HI, AG is 4 mgZ, the detection limit of Hp is 6.5 / £ 3 ⁇ 4, and the detection limit of Tf is 2 rn / Z. is there. Contaminant protein content (m /)
- ⁇ DL indicates a value below the detection limit.
- Example 1 the pH adjustment with 0.8M sodium bicarbonate in the anion exchanger treatment step (2) was adjusted to pH 5.25 and the pH adjustment in the cation exchanger treatment step (3) was adjusted to 5.
- An albumin preparation was prepared in the same manner as in Example 1 except that the preparation was performed at 25.
- the polymer content and the contaminating protein content were measured in the same manner as in Example 1. As a result, the polymer was below the detection limit, and the Hp, aj-AG, and Tf contents were below the detection limit.
- the albumin preparation of the present invention is a preparation excellent in safety, stability and the like, in which the virus is inactivated by the heat treatment, the content of the polymer and the content of contaminating proteins such as transferrin are extremely small.
- the method for producing the albumin preparation of the present invention is a method in which an albumin aqueous solution from which contaminating proteins having various isoelectric points have been removed by treatment with an anion exchanger and a cation exchanger is subjected to heat treatment. Polymerization caused by protein can be suppressed, polymer content and contaminant protein content are low and contamination is a concern. To obtain albumin preparations with inactivated virus
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- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- Animal Behavior & Ethology (AREA)
- Biophysics (AREA)
- Gastroenterology & Hepatology (AREA)
- Zoology (AREA)
- Toxicology (AREA)
- Engineering & Computer Science (AREA)
- Veterinary Medicine (AREA)
- Epidemiology (AREA)
- Genetics & Genomics (AREA)
- Public Health (AREA)
- Biomedical Technology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Immunology (AREA)
- Pharmacology & Pharmacy (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Description
Claims
Priority Applications (4)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
CA002033969A CA2033969C (en) | 1989-06-15 | 1990-06-15 | Albumin preparation and process for producing same |
EP90909363A EP0428758B1 (en) | 1989-06-15 | 1990-06-15 | Method for producing an albumin preparation |
DE69031974T DE69031974T2 (de) | 1989-06-15 | 1990-06-15 | Verfahren zur herstellung einer albuminzubereitung |
KR1019910700176A KR100186824B1 (ko) | 1989-06-15 | 1990-06-15 | 알부민 제제 및 이의 제조방법 |
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP1153137A JPH0768137B2 (ja) | 1989-06-15 | 1989-06-15 | アルブミン製剤及びその製法 |
JP1/153137 | 1989-06-15 |
Publications (1)
Publication Number | Publication Date |
---|---|
WO1990015617A1 true WO1990015617A1 (en) | 1990-12-27 |
Family
ID=15555816
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
PCT/JP1990/000788 WO1990015617A1 (en) | 1989-06-15 | 1990-06-15 | Albumin preparation and method of producing the same |
Country Status (8)
Country | Link |
---|---|
EP (2) | EP0792887A1 (ja) |
JP (1) | JPH0768137B2 (ja) |
KR (1) | KR100186824B1 (ja) |
CA (1) | CA2033969C (ja) |
DE (1) | DE69031974T2 (ja) |
DK (1) | DK0428758T3 (ja) |
ES (1) | ES2111538T3 (ja) |
WO (1) | WO1990015617A1 (ja) |
Cited By (4)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN103880947A (zh) * | 2012-12-21 | 2014-06-25 | 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 |
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 |
US10183984B2 (en) | 2010-12-20 | 2019-01-22 | Healthgen Biotechnology Corp. | Method for extracting recombinant human serum albumin from transgenic rice grain |
US20210100941A1 (en) * | 2017-03-28 | 2021-04-08 | Advitos Gmbh | Compositions and methods for regenerating carrier protein-containing multiple pass albumin dialysis fluid |
Families Citing this family (18)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
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 |
US5849874A (en) * | 1991-07-12 | 1998-12-15 | Gist-Brocades, N.V. | Process for the purification of serum albumin |
JPH06501033A (ja) | 1991-07-12 | 1994-01-27 | ギスト ブロカデス ナムローゼ フェンノートシャップ | 血清アルブミンの精製方法 |
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 |
US5521287A (en) * | 1992-05-20 | 1996-05-28 | The Green Cross Corporation | Recombinant human serum albumin, process for producing the same and pharmaceutical preparation containing the same |
US5728553A (en) * | 1992-09-23 | 1998-03-17 | Delta Biotechnology Limited | High purity albumin and method of producing |
JPH07126182A (ja) * | 1993-10-27 | 1995-05-16 | Green Cross Corp:The | 組換えヒト血清アルブミン製剤の滅菌方法 |
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 |
GB9902000D0 (en) | 1999-01-30 | 1999-03-17 | Delta Biotechnology Ltd | Process |
JP4683810B2 (ja) * | 2000-02-29 | 2011-05-18 | 中外製薬株式会社 | 長期安定化製剤 |
JP4798833B2 (ja) | 2000-10-24 | 2011-10-19 | 一般財団法人化学及血清療法研究所 | 加熱処理工程を含むヒト血清アルブミンの製造方法 |
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 |
ATE414537T1 (de) | 2001-08-29 | 2008-12-15 | Chugai Pharmaceutical Co Ltd | Antikörper enthaltende stabilisierte zubereitungen |
JP2006182649A (ja) * | 2003-04-09 | 2006-07-13 | Chemo Sero Therapeut Res Inst | アルブミン凝集体及び/または不純蛋白質の除去方法 |
ES2543978T3 (es) | 2003-04-09 | 2015-08-26 | The Chemo-Sero-Therapeutic Research Institute | Proceso para la producción de una preparación de albúmina |
US20150343385A1 (en) | 2012-12-14 | 2015-12-03 | General Electric Company | Flat filtration module |
CN104837543B (zh) | 2012-12-14 | 2017-03-08 | 通用电气公司 | 平式反渗透模块及系统 |
US11739166B2 (en) | 2020-07-02 | 2023-08-29 | Davol Inc. | Reactive polysaccharide-based hemostatic agent |
Citations (7)
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JPS5247915A (en) * | 1975-10-09 | 1977-04-16 | Pharmacia Fine Chemicals Ab | Isolation of alubumin from blood article |
JPS56125310A (en) * | 1980-03-07 | 1981-10-01 | Nippon Seiyaku Kk | Preparation of protein solution consisting essentially of lipoprotein of plasma with high specific gravity and serum albumin |
JPS5795997A (en) * | 1980-12-08 | 1982-06-15 | Nippon Sekijiyuujishiya | Removal of admixed protein from albumin-containing solution in presence of water-soluble high polymer |
JPS61194027A (ja) * | 1985-02-25 | 1986-08-28 | Asahi Medical Kk | アルブミン製剤の製造法 |
JPS6288961A (ja) * | 1985-10-16 | 1987-04-23 | Asahi Medical Co Ltd | アルブミンとグロブリンの分離方法 |
JPS6288962A (ja) * | 1985-10-16 | 1987-04-23 | Asahi Medical Co Ltd | クロマトグラフイ−によるアルブミンの短時間分離法 |
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 |
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EP0079739A3 (en) * | 1981-11-12 | 1984-08-08 | The Upjohn Company | Albumin-based nucleotides, their replication and use, and plasmids for use therein |
JPS58185524A (ja) * | 1982-04-24 | 1983-10-29 | Asahi Chem Ind Co Ltd | 液体クロマトグラフイ−による体液成分の分離方法 |
FR2543448A1 (fr) * | 1983-04-01 | 1984-10-05 | Rhone Poulenc Spec Chim | Procede de fractionnement du plasma |
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 |
-
1989
- 1989-06-15 JP JP1153137A patent/JPH0768137B2/ja not_active Expired - Lifetime
-
1990
- 1990-06-15 EP EP97105247A patent/EP0792887A1/en not_active Withdrawn
- 1990-06-15 DK DK90909363.5T patent/DK0428758T3/da active
- 1990-06-15 WO PCT/JP1990/000788 patent/WO1990015617A1/ja active IP Right Grant
- 1990-06-15 CA CA002033969A patent/CA2033969C/en not_active Expired - Fee Related
- 1990-06-15 DE DE69031974T patent/DE69031974T2/de not_active Expired - Fee Related
- 1990-06-15 EP EP90909363A patent/EP0428758B1/en not_active Expired - Lifetime
- 1990-06-15 KR KR1019910700176A patent/KR100186824B1/ko not_active IP Right Cessation
- 1990-06-15 ES ES90909363T patent/ES2111538T3/es not_active Expired - Lifetime
Patent Citations (7)
Publication number | Priority date | Publication date | Assignee | Title |
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JPS5247915A (en) * | 1975-10-09 | 1977-04-16 | Pharmacia Fine Chemicals Ab | Isolation of alubumin from blood article |
JPS56125310A (en) * | 1980-03-07 | 1981-10-01 | Nippon Seiyaku Kk | Preparation of protein solution consisting essentially of lipoprotein of plasma with high specific gravity and serum albumin |
JPS5795997A (en) * | 1980-12-08 | 1982-06-15 | Nippon Sekijiyuujishiya | Removal of admixed protein from albumin-containing solution in presence of water-soluble high polymer |
JPS61194027A (ja) * | 1985-02-25 | 1986-08-28 | Asahi Medical Kk | アルブミン製剤の製造法 |
JPS6288961A (ja) * | 1985-10-16 | 1987-04-23 | Asahi Medical Co Ltd | アルブミンとグロブリンの分離方法 |
JPS6288962A (ja) * | 1985-10-16 | 1987-04-23 | Asahi Medical Co Ltd | クロマトグラフイ−によるアルブミンの短時間分離法 |
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 |
Non-Patent Citations (1)
Title |
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Cited By (7)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US10183984B2 (en) | 2010-12-20 | 2019-01-22 | Healthgen Biotechnology Corp. | Method for extracting recombinant 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 |
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 |
CN103880947A (zh) * | 2012-12-21 | 2014-06-25 | 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 |
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 |
US10730926B2 (en) | 2012-12-21 | 2020-08-04 | Wuhan Healthgen Biotechnology Corp | Chromatographic method for isolating and purifying high-purity recombined human serum albumin |
US20210100941A1 (en) * | 2017-03-28 | 2021-04-08 | Advitos Gmbh | Compositions and methods for regenerating carrier protein-containing multiple pass albumin dialysis fluid |
Also Published As
Publication number | Publication date |
---|---|
DK0428758T3 (da) | 1998-03-16 |
EP0792887A1 (en) | 1997-09-03 |
CA2033969C (en) | 2002-10-29 |
DE69031974T2 (de) | 1998-06-04 |
JPH0768137B2 (ja) | 1995-07-26 |
EP0428758A1 (en) | 1991-05-29 |
EP0428758B1 (en) | 1998-01-21 |
KR100186824B1 (ko) | 1999-05-01 |
CA2033969A1 (en) | 1990-12-16 |
ES2111538T3 (es) | 1998-03-16 |
JPH0317023A (ja) | 1991-01-25 |
DE69031974D1 (de) | 1998-02-26 |
KR920700043A (ko) | 1992-02-19 |
EP0428758A4 (en) | 1992-04-15 |
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