重组枯草杆菌纤溶酶的酶学性质研究  

Enzymatic Characterization of a Recombinant Fibrinolytic Enzyme from Bacillus sp.N18

作　　者：卞慧芳[1] 黄静[1] 左翼[1] 郁正艳[1] 吴自荣[1] 

机构地区：[1]华东师范大学生命科学学院,上海200062

出　　处：《中国生物工程杂志》2004年第10期81-84,共4页China Biotechnology

基　　金：上海市科委资助项目 (985 4190 0 0 3 )

摘　　要：对一种重组枯草杆菌纤溶酶 (rBSFE)的酶学性质进行了初步研究 ,结果表明 :酶作用最适温度为 35℃ ;最适反应pH为 8 0 ;酶活性能被PMSF抑制 ,是典型的丝氨酸蛋白酶。通过与尿激酶进行比较 ,发现该酶对纤维蛋白有直接降解作用 ,而对于纤维蛋白原的敏感性则低于尿激酶 ,提示该酶具有直接溶栓作用 ,又不致引起出血 ,是一种有潜力的新型溶栓剂。Enzymatic characterization of a recombinant Bacillus subtilis fibrinolytic enzyme (rBSFE) was studied. The optimal temperature and pH of rBSFE is 35℃ and 8 0, respectively. PMSF is the enzyme's specific inhibitor which demonstrates that rBSFE is a typical serine protease. The results also suggest that rBSFE is less sensitive on the cleavage of fibrinogen, but is more sensitive on the cleavage of cross linked fibrin as compared to Urokinase. The current study indicated that rBSFE could cleave directly cross linked fibrin without bleeding complications and could be used as a potent thrombolytic agent.

关 键 词：尿激酶 纤溶酶 纤维蛋白原 溶栓作用 出血 溶栓剂 枯草杆菌 酶学性质 最适温度 丝氨酸蛋白酶 

分 类 号：Q556[生物学—生物化学] R743[医药卫生—神经病学与精神病学]