Fibrin-Specific Fibrinolysis Induced by Recombinant Staphylokinase
| Autor: | Teruo Yokokura, Syusuke Hashimoto, Yoshiyuki Shishido, Masashi Sakai, Norimasa Kaneda, Tsuneo Matsumoto, Hiroshi Sansawa, Kisaku Shimura |
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| Rok vydání: | 1994 |
| Předmět: |
Male
Plasmin Streptokinase medicine.medical_treatment Pharmaceutical Science Pharmacology Tissue plasminogen activator Fibrin Iodine Radioisotopes Fibrinolysis medicine Animals Humans biology Chemistry T-plasminogen activator Fibrinogen Metalloendopeptidases Plasminogen Thrombosis Staphylokinase General Medicine Chromatography Ion Exchange Recombinant Proteins Biochemistry Tissue Plasminogen Activator biology.protein Rabbits Jugular Veins Plasminogen activator medicine.drug |
| Zdroj: | Biological and Pharmaceutical Bulletin. 17:1060-1064 |
| ISSN: | 1347-5215 0918-6158 |
| Popis: | We compared the thrombolytic properties of recombinant staphylokinase (SAK) with those of streptokinase (SK), a tissue-type plasminogen activator (t-PA) and a urokinase-type plasminogen activator (u-PA) in the jugular vein thrombosis model in the rabbit in vivo and a circulating human plasma system in vitro. 50% thrombolysis was observed at 360 min after intravenous infusion into rabbits of 150 micrograms/kg of SAK or 500 micrograms/kg of t-PA, respectively. And the fibrinogen level in the blood was not affected by either agent. 50% clot lysis in vitro was observed at 120 min with 1.8 micrograms/ml of SAK, 22.1 micrograms/ml of SK, 2.1 micrograms/ml of t-PA, or 4.7 micrograms/ml of u-PA, respectively. All the plasminogen activators with the exception of SAK decreased the residual fibrinogen level in the circulating plasma at their moderate concentration for clot lysis. SAK had less influence on the plasminogen and alpha 2-plasmin inhibitor (alpha 2-antiplasmin) levels than the other plasminogen activators. These findings suggest that SAK is a potent fibrin-specific thrombolytic agent. |
| Databáze: | OpenAIRE |
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