Biomolecules & Therapeutics

  • 제3권2호
  • /
  • Pages.159-164
  • /
  • 1995
  • /
  • 1976-9148(pISSN)
  • /
  • 2005-4483(eISSN)
한국응용약물학회 (The Korean Society of Applied Pharmacology)
권호 표지

한국 독사독으로부터의 혈전 용해제 개발에 관한 연구 I. 살모사(A. bromhoffi brevicaudus) 사독 Protease의 정제에 관한 연구

Studies on the Development of a Thrombolytic Agent from Korean Snake Venom I. Purification of a Protease from the Venom of A. bromhoffi brevicaudus

  • 이문한 (서울대학교 수의과대학) ;
  • 김병재 (서울대학교 수의과대학) ;
  • 임종섭 (존스홉킨스 의과대학) ;
  • 이항 (서울대학교 수의과대학) ;
  • 이혜숙 (서울대학교 수의과대학) ;
  • 김종호 (서울대학교 수의과대학) ;
  • 채창수 (서울대학교 수의과대학)
  • Lee, Mun-Han (College of Veterinary Medicine, Seoul National University) ;
  • Kim, Byoung-Jae (College of Veterinary Medicine, Seoul National University) ;
  • Rim, Jong-Seop (Depart. of Physiol, School of Medicine, Johns Hopkins University) ;
  • Lee, Hang (College of Veterinary Medicine, Seoul National University) ;
  • Lee, Hye-Suk (College of Veterinary Medicine, Seoul National University) ;
  • Kim, Jong-Ho (College of Veterinary Medicine, Seoul National University) ;
  • Chai, Chang-Su (College of Veterinary Medicine, Seoul National University)
  • 발행 : 1995.06.01
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초록

Fibrinolytic and fibrinogenolytic activities of the venoms from the Korean snakes, Agkistrodon caliginosus, nosus, 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(open)olytic activity was purified by p-amino-benzamidine affinity chromatography and DEAE ion-exchange chromatography. The purified enzyme had a molecular weight of 50,800 and a capability to degrade the B$\beta$-chain of fibrinogen preferentially to the $A\alpha$-chain, but not the ${\gamma}$-chain. Fibrinolytic activity of the purified enzyme was approximately 3.8 plasmin unit/mg protein.

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