CA1301680C - Mode de preparation de solutions proteiniques physiologiquement actives - Google Patents

Mode de preparation de solutions proteiniques physiologiquement actives

Info

Publication number: CA1301680C
Authority: CA; Canada
Prior art keywords: human; solution; filter; substance; active substance
Prior art date: 1986-01-20
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.): Expired - Lifetime

Application number

CA000524341A

Other languages

English (en)

Inventor

Hajime Hiratani

Jun Tateishi

Tetsuyuki Kitamoto

Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)

Japan Chemical Research Co Ltd

Original Assignee

Japan Chemical Research Co Ltd

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

1986-01-20

Filing date

1986-12-02

Publication date

1992-05-26

1986-01-20 Priority claimed from JP61009811A external-priority patent/JPH0720986B2/ja

1986-12-02 Application filed by Japan Chemical Research Co Ltd filed Critical Japan Chemical Research Co Ltd

1992-05-26 Application granted granted Critical

1992-05-26 Publication of CA1301680C publication Critical patent/CA1301680C/fr

2009-05-26 Anticipated expiration legal-status Critical

Status Expired - Lifetime legal-status Critical Current

Links

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239000013543 active substance Substances 0.000 claims abstract description 29
238000001914 filtration Methods 0.000 claims abstract description 21
239000000126 substance Substances 0.000 claims abstract description 21
102000002265 Human Growth Hormone Human genes 0.000 claims abstract description 16
108010000521 Human Growth Hormone Proteins 0.000 claims abstract description 16
239000000854 Human Growth Hormone Substances 0.000 claims abstract description 16
241000700605 Viruses Species 0.000 claims abstract description 12
239000011148 porous material Substances 0.000 claims abstract description 12
108010010803 Gelatin Proteins 0.000 claims abstract description 10
239000008273 gelatin Substances 0.000 claims abstract description 10
229920000159 gelatin Polymers 0.000 claims abstract description 10
235000019322 gelatine Nutrition 0.000 claims abstract description 10
235000011852 gelatine desserts Nutrition 0.000 claims abstract description 10
102000001399 Kallikrein Human genes 0.000 claims abstract description 6
108060005987 Kallikrein Proteins 0.000 claims abstract description 6
229940122618 Trypsin inhibitor Drugs 0.000 claims abstract description 6
101710162629 Trypsin inhibitor Proteins 0.000 claims abstract description 6
239000002753 trypsin inhibitor Substances 0.000 claims abstract description 6
239000001267 polyvinylpyrrolidone Substances 0.000 claims abstract description 4
229920000036 polyvinylpyrrolidone Polymers 0.000 claims abstract description 4
235000013855 polyvinylpyrrolidone Nutrition 0.000 claims abstract description 4
102000008100 Human Serum Albumin Human genes 0.000 claims description 11
108091006905 Human Serum Albumin Proteins 0.000 claims description 11
102000003990 Urokinase-type plasminogen activator Human genes 0.000 claims description 8
108090000435 Urokinase-type plasminogen activator Proteins 0.000 claims description 8
229960005356 urokinase Drugs 0.000 claims description 8
239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 claims description 7
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108010086677 Gonadotropins Proteins 0.000 claims description 4
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VBEQCZHXXJYVRD-GACYYNSASA-N uroanthelone Chemical compound C([C@@H](C(=O)N[C@H](C(=O)N[C@@H](CS)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CS)C(=O)N[C@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)NCC(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O)C(C)C)[C@@H](C)O)NC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CCSC)NC(=O)[C@H](CS)NC(=O)[C@@H](NC(=O)CNC(=O)CNC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CS)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CS)NC(=O)CNC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC(N)=O)C(C)C)[C@@H](C)CC)C1=CC=C(O)C=C1 VBEQCZHXXJYVRD-GACYYNSASA-N 0.000 abstract description 3
102000009027 Albumins Human genes 0.000 abstract description 2
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108010050904 Interferons Proteins 0.000 abstract description 2
229940079322 interferon Drugs 0.000 abstract description 2
208000003407 Creutzfeldt-Jakob Syndrome Diseases 0.000 abstract 1
244000052769 pathogen Species 0.000 abstract 1
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LYCAIKOWRPUZTN-UHFFFAOYSA-N Ethylene glycol Chemical compound OCCO LYCAIKOWRPUZTN-UHFFFAOYSA-N 0.000 description 6
239000000706 filtrate Substances 0.000 description 6
210000004369 blood Anatomy 0.000 description 5
239000008280 blood Substances 0.000 description 5
238000003127 radioimmunoassay Methods 0.000 description 5
210000001835 viscera Anatomy 0.000 description 5
LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 4
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208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 4
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239000004475 Arginine Substances 0.000 description 3
108060003951 Immunoglobulin Proteins 0.000 description 3
229920001030 Polyethylene Glycol 4000 Polymers 0.000 description 3
229920001213 Polysorbate 20 Polymers 0.000 description 3
239000007864 aqueous solution Substances 0.000 description 3
ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 3
239000011248 coating agent Substances 0.000 description 3
238000000576 coating method Methods 0.000 description 3
239000005556 hormone Substances 0.000 description 3
229940088597 hormone Drugs 0.000 description 3
102000018358 immunoglobulin Human genes 0.000 description 3
239000000203 mixture Substances 0.000 description 3
VZSRBBMJRBPUNF-UHFFFAOYSA-N 2-(2,3-dihydro-1H-inden-2-ylamino)-N-[3-oxo-3-(2,4,6,7-tetrahydrotriazolo[4,5-c]pyridin-5-yl)propyl]pyrimidine-5-carboxamide Chemical compound C1C(CC2=CC=CC=C12)NC1=NC=C(C=N1)C(=O)NCCC(N1CC2=C(CC1)NN=N2)=O VZSRBBMJRBPUNF-UHFFFAOYSA-N 0.000 description 2
HEDRZPFGACZZDS-UHFFFAOYSA-N Chloroform Chemical compound ClC(Cl)Cl HEDRZPFGACZZDS-UHFFFAOYSA-N 0.000 description 2
WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 2
102000018997 Growth Hormone Human genes 0.000 description 2
108010051696 Growth Hormone Proteins 0.000 description 2
108010002885 Polygeline Proteins 0.000 description 2
102000007562 Serum Albumin Human genes 0.000 description 2
108010071390 Serum Albumin Proteins 0.000 description 2
210000004556 brain Anatomy 0.000 description 2
210000003710 cerebral cortex Anatomy 0.000 description 2
238000011109 contamination Methods 0.000 description 2
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229920001451 polypropylene glycol Polymers 0.000 description 2
238000002360 preparation method Methods 0.000 description 2
239000007858 starting material Substances 0.000 description 2
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HMUNWXXNJPVALC-UHFFFAOYSA-N 1-[4-[2-(2,3-dihydro-1H-inden-2-ylamino)pyrimidin-5-yl]piperazin-1-yl]-2-(2,4,6,7-tetrahydrotriazolo[4,5-c]pyridin-5-yl)ethanone Chemical compound C1C(CC2=CC=CC=C12)NC1=NC=C(C=N1)N1CCN(CC1)C(CN1CC2=C(CC1)NN=N2)=O HMUNWXXNJPVALC-UHFFFAOYSA-N 0.000 description 1
ZCYVEMRRCGMTRW-UHFFFAOYSA-N 7553-56-2 Chemical compound [I] ZCYVEMRRCGMTRW-UHFFFAOYSA-N 0.000 description 1
206010013883 Dwarfism Diseases 0.000 description 1
102000004190 Enzymes Human genes 0.000 description 1
108090000790 Enzymes Proteins 0.000 description 1
SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 description 1
VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 1
MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 1
241000699666 Mus <mouse, genus> Species 0.000 description 1
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MMPOTNFPDMJTRR-UHFFFAOYSA-N OOOOOOOOOOO Chemical compound OOOOOOOOOOO MMPOTNFPDMJTRR-UHFFFAOYSA-N 0.000 description 1
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 1
102000004142 Trypsin Human genes 0.000 description 1
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238000004458 analytical method Methods 0.000 description 1
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229910052740 iodine Inorganic materials 0.000 description 1
239000011630 iodine Substances 0.000 description 1
210000000265 leukocyte Anatomy 0.000 description 1
125000002496 methyl group Chemical group [H]C([H])([H])* 0.000 description 1
210000000653 nervous system Anatomy 0.000 description 1
230000007171 neuropathology Effects 0.000 description 1
230000001575 pathological effect Effects 0.000 description 1
208000003068 pituitary dwarfism Diseases 0.000 description 1
230000001817 pituitary effect Effects 0.000 description 1
229920002401 polyacrylamide Polymers 0.000 description 1
229940057838 polyethylene glycol 4000 Drugs 0.000 description 1
239000012286 potassium permanganate Substances 0.000 description 1
239000000843 powder Substances 0.000 description 1
238000001556 precipitation Methods 0.000 description 1
238000009877 rendering Methods 0.000 description 1
210000002966 serum Anatomy 0.000 description 1
239000011780 sodium chloride Substances 0.000 description 1
SUKJFIGYRHOWBL-UHFFFAOYSA-N sodium hypochlorite Chemical compound [Na+].Cl[O-] SUKJFIGYRHOWBL-UHFFFAOYSA-N 0.000 description 1
239000000758 substrate Substances 0.000 description 1
230000001629 suppression Effects 0.000 description 1
208000024891 symptom Diseases 0.000 description 1
239000012588 trypsin Substances 0.000 description 1
238000005406 washing Methods 0.000 description 1
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1

Landscapes

Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Peptides Or Proteins (AREA)

CA000524341A 1986-01-20 1986-12-02 Mode de preparation de solutions proteiniques physiologiquement actives Expired - Lifetime CA1301680C (fr)

Applications Claiming Priority (2)

Application Number	Priority Date	Filing Date	Title
JP61009811A JPH0720986B2 (ja)	1985-10-07	1986-01-20	生理活性物質の製造法
JP9811/86		1986-01-20

Publications (1)

Publication Number	Publication Date
CA1301680C true CA1301680C (fr)	1992-05-26

Family

ID=11730549

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
CA000524341A Expired - Lifetime CA1301680C (fr)	1986-01-20	1986-12-02	Mode de preparation de solutions proteiniques physiologiquement actives

Country Status (1)

Country	Link
CA (1)	CA1301680C (fr)

1986
- 1986-12-02 CA CA000524341A patent/CA1301680C/fr not_active Expired - Lifetime

Legal Events

Date	Code	Title	Description
2004-05-26	MKLA	Lapsed

Publication	Publication Date	Title
RU2337109C2 (ru)	2008-10-27	ПРЕПАРАТ ИММУНОГЛОБУЛИНА IgG И СПОСОБ ЕГО ПОЛУЧЕНИЯ
CA2192683C (fr)	2005-07-05	Filtration
US4605394A (en)	1986-08-12	Methods for the treatment of pathological conditions by removing interferon from the organism
DE69332268T2 (de)	2003-08-14	Verfahren zur herstellung von rekombinant mhcii protein in mikroorganismen
DE3886249T2 (de)	1994-06-30	Verfahren zur Ultrareinigung von Faktor VIII:C.
EP0447585B2 (fr)	2003-05-07	Procédé de production d'une préparation tolérante d'immunoglobuline G intraveineuse
US4482485A (en)	1984-11-13	Method of preparation of human urine origin colony-stimulating factor and kallikrein
ATE225368T1 (de)	2002-10-15	Verfahren zur reinigung von faktor viii
RU2097047C1 (ru)	1997-11-27	Препарат человеческого фактора xi свертывания крови и способ его получения
EP0469985A1 (fr)	1992-02-05	Procédé de fabrication de facteur Von Willebrand ayant une très haute pureté
EP0567448B2 (fr)	2005-01-05	Préparation de facteur VIII
JPH06321994A (ja)	1994-11-22	アンチトロンビン調製物およびその調製方法
US5173415A (en)	1992-12-22	Process for removal of viruses from solutions of physiologically active substances
EP0825998B1 (fr)	2003-04-09	Preparation de l'immunoglobuline
EP0994722B1 (fr)	2006-01-18	Procede permettant d'eliminer l'endotoxine contenue dans des vaccins
EP0138167A1 (fr)	1985-04-24	Méthode de purification d'HBs antigène
RU2148411C1 (ru)	2000-05-10	Способ получения с помощью хроматографических методов вирусно-инактивированной фракции, содержащей фактор viii
EP0219295B1 (fr)	1994-01-19	Procédé de production de l'hormone de croissance humaine
SK174799A3 (en)	2000-07-11	Process for reducing the concentration of viral and molecular pathogens in a biological material
JPH07155194A (ja)	1995-06-20	タンパク質の精製法
US6372510B1 (en)	2002-04-16	Method for removing unconventional transmissible agents from a protein solution
JPH0114788B2 (fr)	1989-03-14
JPH01135725A (ja)	1989-05-29	抗−ｐＨ不安定アルフアインターフエロン抗体の製造方法
JPH02304030A (ja)	1990-12-17	抗ｎａｎｂウイルス抗体陽性静注用免疫グロブリン製剤の製造方法
de Lille	1997	Burnouf-Radosevich et a