동백나무 추출물의 혈전용해 효소활성

Abstract

The fibrinolytic activities of soluble proteins extracted from young leaves of Camellia japonica L. were studied. Fibrinolytic activity of extract from partitions of C. japonica L. showed 1.6-2.0 times higher than plasmin used as positive control. The fibrinolytic enzyme was confirmed directly from young leaves of C. japonica L. by a fibrin plate and fibrin zymography. The protein was composed of a single polypeptide and its apparent molecular weight was found to be 45 kDa, as judged by SDS-polyacrylamide gel electrophoresis. The optimum pH and temperature for the fibrinolytic activity were pH 5.5 and 30℃, respectively. Also, the fibrinolytic activity was clearly inhibited by PMSF and TLCK, suggesting that it is a member of the trypsin-like serine protease. All these results suggest the protease is a fibrinolytic enzyme belong to a family of trypsin-like serine protease.