JPH0462302B2 - - Google Patents
Info
- Publication number
- JPH0462302B2 JPH0462302B2 JP60079429A JP7942985A JPH0462302B2 JP H0462302 B2 JPH0462302 B2 JP H0462302B2 JP 60079429 A JP60079429 A JP 60079429A JP 7942985 A JP7942985 A JP 7942985A JP H0462302 B2 JPH0462302 B2 JP H0462302B2
- Authority
- JP
- Japan
- Prior art keywords
- urokinase
- precursor
- urokinase precursor
- albumin
- present
- Prior art date
- 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
Links
- 229960005356 urokinase Drugs 0.000 claims description 39
- 102000003990 Urokinase-type plasminogen activator Human genes 0.000 claims description 38
- 108090000435 Urokinase-type plasminogen activator Proteins 0.000 claims description 38
- 239000002243 precursor Substances 0.000 claims description 37
- 102000008100 Human Serum Albumin Human genes 0.000 claims description 14
- 108091006905 Human Serum Albumin Proteins 0.000 claims description 14
- 235000001014 amino acid Nutrition 0.000 claims description 8
- 150000001413 amino acids Chemical class 0.000 claims description 8
- 150000003839 salts Chemical class 0.000 claims description 8
- 239000004475 Arginine Substances 0.000 claims description 7
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 claims description 7
- 238000002360 preparation method Methods 0.000 claims description 6
- 239000003381 stabilizer Substances 0.000 claims description 6
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 claims description 2
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 claims description 2
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 claims description 2
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 claims description 2
- 239000004472 Lysine Substances 0.000 claims description 2
- 235000013922 glutamic acid Nutrition 0.000 claims description 2
- 239000004220 glutamic acid Substances 0.000 claims description 2
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 claims description 2
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 claims 1
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 claims 1
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 claims 1
- 235000003704 aspartic acid Nutrition 0.000 claims 1
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 claims 1
- 230000000694 effects Effects 0.000 description 13
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 6
- 229940024606 amino acid Drugs 0.000 description 6
- 229960003121 arginine Drugs 0.000 description 6
- 239000008363 phosphate buffer Substances 0.000 description 6
- 102000009027 Albumins Human genes 0.000 description 5
- 108010088751 Albumins Proteins 0.000 description 5
- 229940012957 plasmin Drugs 0.000 description 5
- 208000007536 Thrombosis Diseases 0.000 description 4
- 235000018102 proteins Nutrition 0.000 description 4
- 102000004169 proteins and genes Human genes 0.000 description 4
- 108090000623 proteins and genes Proteins 0.000 description 4
- 238000009472 formulation Methods 0.000 description 3
- 210000003292 kidney cell Anatomy 0.000 description 3
- 238000000034 method Methods 0.000 description 3
- 239000000203 mixture Substances 0.000 description 3
- LPUQAYUQRXPFSQ-DFWYDOINSA-M monosodium L-glutamate Chemical compound [Na+].[O-]C(=O)[C@@H](N)CCC(O)=O LPUQAYUQRXPFSQ-DFWYDOINSA-M 0.000 description 3
- 235000013923 monosodium glutamate Nutrition 0.000 description 3
- 239000011780 sodium chloride Substances 0.000 description 3
- 238000003860 storage Methods 0.000 description 3
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 2
- 102000009123 Fibrin Human genes 0.000 description 2
- 108010073385 Fibrin Proteins 0.000 description 2
- BWGVNKXGVNDBDI-UHFFFAOYSA-N Fibrin monomer Chemical compound CNC(=O)CNC(=O)CN BWGVNKXGVNDBDI-UHFFFAOYSA-N 0.000 description 2
- 210000004027 cell Anatomy 0.000 description 2
- 229950003499 fibrin Drugs 0.000 description 2
- 238000004108 freeze drying Methods 0.000 description 2
- 239000001963 growth medium Substances 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 229940073490 sodium glutamate Drugs 0.000 description 2
- 239000002904 solvent Substances 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- SUUWYOYAXFUOLX-ZBRNBAAYSA-N (2s)-2-aminobutanedioic acid;(2s)-2-amino-5-(diaminomethylideneamino)pentanoic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O.OC(=O)[C@@H](N)CCCN=C(N)N SUUWYOYAXFUOLX-ZBRNBAAYSA-N 0.000 description 1
- NHBKXEKEPDILRR-UHFFFAOYSA-N 2,3-bis(butanoylsulfanyl)propyl butanoate Chemical compound CCCC(=O)OCC(SC(=O)CCC)CSC(=O)CCC NHBKXEKEPDILRR-UHFFFAOYSA-N 0.000 description 1
- IVLXQGJVBGMLRR-UHFFFAOYSA-N 2-aminoacetic acid;hydron;chloride Chemical compound Cl.NCC(O)=O IVLXQGJVBGMLRR-UHFFFAOYSA-N 0.000 description 1
- 208000005189 Embolism Diseases 0.000 description 1
- 102000008946 Fibrinogen Human genes 0.000 description 1
- 108010049003 Fibrinogen Proteins 0.000 description 1
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 206010035226 Plasma cell myeloma Diseases 0.000 description 1
- 239000002202 Polyethylene glycol Substances 0.000 description 1
- 229920005654 Sephadex Polymers 0.000 description 1
- 239000012507 Sephadex™ Substances 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 239000000654 additive Substances 0.000 description 1
- 229960002223 arginine aspartate Drugs 0.000 description 1
- 239000000872 buffer Substances 0.000 description 1
- 239000012228 culture supernatant Substances 0.000 description 1
- ATDGTVJJHBUTRL-UHFFFAOYSA-N cyanogen bromide Chemical compound BrC#N ATDGTVJJHBUTRL-UHFFFAOYSA-N 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 229940012952 fibrinogen Drugs 0.000 description 1
- 230000020764 fibrinolysis Effects 0.000 description 1
- 239000000706 filtrate Substances 0.000 description 1
- 238000005194 fractionation Methods 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 208000006454 hepatitis Diseases 0.000 description 1
- 231100000283 hepatitis Toxicity 0.000 description 1
- 210000004408 hybridoma Anatomy 0.000 description 1
- 230000016784 immunoglobulin production Effects 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 239000004223 monosodium glutamate Substances 0.000 description 1
- 201000000050 myeloid neoplasm Diseases 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 230000003472 neutralizing effect Effects 0.000 description 1
- 150000007524 organic acids Chemical class 0.000 description 1
- 229920001223 polyethylene glycol Polymers 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 235000019833 protease Nutrition 0.000 description 1
- 239000012264 purified product Substances 0.000 description 1
- 239000004017 serum-free culture medium Substances 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 210000004989 spleen cell Anatomy 0.000 description 1
- 238000011146 sterile filtration Methods 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 229940124597 therapeutic agent Drugs 0.000 description 1
- 210000002700 urine Anatomy 0.000 description 1
- 230000002792 vascular Effects 0.000 description 1
Landscapes
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Priority Applications (6)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP60079429A JPS61238732A (ja) | 1985-04-16 | 1985-04-16 | ウロキナーゼ前駆体乾燥製剤 |
CA000506647A CA1336585C (fr) | 1985-04-16 | 1986-04-15 | Methode de stabilisation du precurseur de l'urokinose et preparation contenant ce precurseur |
KR1019860002879A KR940003056B1 (ko) | 1985-04-16 | 1986-04-15 | 우로키나제 전구체를 안정화시키는 방법 |
EP86105235A EP0200966B1 (fr) | 1985-04-16 | 1986-04-16 | Méthode de stabilisation d'un précurseur d'urokinase et préparation sèche contenant ce précurseur |
ES554477A ES8706821A1 (es) | 1985-04-16 | 1986-04-16 | Metodo de estabilizar un precursor de uroquinasa |
DE86105235T DE3688713T2 (de) | 1985-04-16 | 1986-04-16 | Verfahren zur Stabilisierung eines Urokinasevorläufers und diesen Vorläufer enthaltendes trockenes Präparat. |
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP60079429A JPS61238732A (ja) | 1985-04-16 | 1985-04-16 | ウロキナーゼ前駆体乾燥製剤 |
Publications (2)
Publication Number | Publication Date |
---|---|
JPS61238732A JPS61238732A (ja) | 1986-10-24 |
JPH0462302B2 true JPH0462302B2 (fr) | 1992-10-05 |
Family
ID=13689627
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP60079429A Granted JPS61238732A (ja) | 1985-04-16 | 1985-04-16 | ウロキナーゼ前駆体乾燥製剤 |
Country Status (1)
Country | Link |
---|---|
JP (1) | JPS61238732A (fr) |
Families Citing this family (4)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPS63174934A (ja) * | 1987-01-13 | 1988-07-19 | Green Cross Corp:The | ウロキナ−ゼ前駆体乾燥製剤 |
US8545459B2 (en) | 2009-02-25 | 2013-10-01 | Teleflex Medical Incorporated | Stabilized enzyme compositions |
US9333280B2 (en) | 2009-02-25 | 2016-05-10 | Teleflex Medical Incorporated | Stabilized enzyme compositions |
WO2015048619A2 (fr) | 2013-09-30 | 2015-04-02 | Teleflex Medical Incorporated | Compositions d'enzymes stabilisées |
Citations (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPS54147916A (en) * | 1978-05-12 | 1979-11-19 | Sumitomo Chem Co Ltd | Preparation of urokinase injection |
-
1985
- 1985-04-16 JP JP60079429A patent/JPS61238732A/ja active Granted
Patent Citations (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPS54147916A (en) * | 1978-05-12 | 1979-11-19 | Sumitomo Chem Co Ltd | Preparation of urokinase injection |
Also Published As
Publication number | Publication date |
---|---|
JPS61238732A (ja) | 1986-10-24 |
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