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초록
We purified and biochemically characterized a fibrinolytic enzyme from the body of a Korean polychaeta, Periserrula leucophryna. This enzyme was identified as serine protease belonging to the trypsin family on the basis of inhibition profile and P1 site specificity on chromogenic substrates SDS-PAGE and FPLC studies showed the protease to have a molecular mass of 28 kDa. The enzyme showed no thrombin-like activity and factor Xa activity (prothrombin activator activity).
- 제목
- 갯지렁이로부터 피브린 효소에 대한 정제 및 생화학적 특성
- 제목 (타언어)
- Purification and Biochmical Characterization of Fibrinolytic Enzyme from the Korean Polychaeta, Periserrula leucophryna
- 저자
- CHANG, CHUNG SOON
- 학회명
- The Biochemical Society of the Republic of Korea