Purification and Characterization of Fibrinolytic Enzyme from Armillariella mellea

뽕나무버섯으로부터 Fibrinolytic enzyme의 정제 및 특성 연구

  • Kim, Jun-Ho (Department of Chemistry, Sang Ji University) ;
  • Kim, Yang-Sun (College of General Education, Semyoung University)
  • 김준호 (상지대학교 이공과대학 화학과) ;
  • 김양선 (세명대학교 교양학부)
  • Published : 1998.12.30


A fibrinolytic enzyme has been isolated from the edible honey mushroom, Armillariella mellea and purified. The apparent molecular mass of purified enzyme was estimated to be 19800Da by SDS polyacryl amide gel electrophoresis and 19900Da by gel filtration, indicating that it was a monomer. The enzyme was optimal at pH 7, suggesting that the purified enzyme was a neutral proteinase. It shows the maximum fibrinolytic activity at $55^{\circ}C$, is completely inactivated above $65^{\circ}C$, and still indicates 40% of activity at $37^{\circ}C$. The fibrinolytic activity has been decreased by the addition of EDTA. Fifteen amino acid sequence was determined by protein sequencing techniques.


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