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한국 독사독으로부터의 혈전 용해제 개발에 관한 연구 1. 살모사 ( A. bromhoffi brevicaudus ) 사독 Protease 의 정제에 관한 연구
이문한(Mun Han Lee),김병재(Byoung Jae KIm),임종섭(Jong Seop Rim),이항(Hang Lee),이혜숙(Hye Suk Lee),김종호(Jong Ho Kim),채창수(Chang Su Chai) 한국응용약물학회 1995 Biomolecules & Therapeutics(구 응용약물학회지) Vol.3 No.2
Fibrinolytic and fibrinogenolytic activities of the venoms from the Korean snakes, Agkistrodon caliginosus, Agkistrodon saxatilis and Agkistrodon blomhoffi brevicaudus were compared by fibrin-plate method and polyacrylamide gel electrophoresis, respectively. The venom from A. blomhoffi brevicaudus showed the highest degree of fibrin(ogen)olytic activity, and a protease with the fibrin(ogen)olytic activity was purified by p-aminobenzamidine affinity chromatography and DEAF ion-exchange chromatography. The purified enzyme had a molecular weight of 50,800 and a capability to degrade the Bβ-chain of fibrinogen preferentially to the Aα-chain, but not the γ-chain. Fibrinolytic activity of the purified enzyme was approximately 3.8 plasmin unit/mg protein.
한국 독사독으로부터의 혈전 용해제 개발에 관한 연구 2. 살모사 ( A. bromhoffi brevicaudus ) 사독 Protease 의 특성과 혈전 용해능에 관한 연구
김병재(Byoung Jae KIm),이문한(Mun Han Lee),임종섭(Jong Seop Rim),이항(Hang Lee),이혜숙(Hye Suk Lee),김종호(Jong Ho Kim),채창수(Chang Su Chai) 한국응용약물학회 1995 Biomolecules & Therapeutics(구 응용약물학회지) Vol.3 No.2
The biochemical properties of the fibrinolytic protease of 50,800 Da isolated from the venom of Agkistrodon blomhoffi brevicaudus were characterized. The enzyme hydrolyzed the carboxyl side of arginine in the synthetic chromogenic peptides, N-Benzoyl-Phe-Val-Arg-pNA and N p-Tosyl-Gly-Pro-Arg-pNA, and the enzyme activity was inhibited by phenylmethylsulfonylfluoride indicating that the enzyme belongs to the serine protease family. The protease showed maximum activity at pH 7.5 and inhibited by ZnCl₂, CuSO₄, but not by soybean trypsin inhibitor, pepstatin A, 2-mercaptoethanol and EDTA. The Km value determined with Np-Tosyl-Gly-Pro-Arg-pNA was 0.2 mM. The thrombolytic activity of the purified enzyme was evaluated by platelet aggregation test in rabbits. While the platelet count ratio in blood of the rabbits injected with thrombin alone declined from 1.0 to 0.6 within 7 min and maintained around 0.6 for 24 hours thereafter, the ratio rapidly recovered from around 0.6 to 0.8 in 1 hr, to 1.0 in 24 hrs when the rabbits were sequentially treated with thrombin and the purified enzyme. The result showed that the serine protease from A. blomhoffi brevicoudus of 50,800 Da had a thrombolytic activity in vivo and the enzyme might be developed as a therapuetic agent for the treatment of thrombic disease.