沙蚕纤溶酶的一种纯化方法

Purification of fibrinolytic enzyme from Perinereis aibuhitensis

目的 从双齿围沙蚕体内提取并纯化一种新的纤溶酶。方法 应用硫酸铵沉淀、透析、凝胶柱层析(Sephadex G- 10 0 )以及电泳等生化手段对沙蚕纤溶酶进行分离纯化。用平板法测定它降解纤维蛋白的活性。结果 得到纯的沙蚕纤溶酶 ,测出其等电点为 4.5左右 ,由两条肽链组成 ,其相对分子量分别为 33 0 0 0 u和 144 0 0 u。结论 该酶为首次从沙蚕中发现的一种新的纤溶酶。

Object To extract and purify a novel fibrinolytic enzyme from Perinereis aibuhitensis Grube Methods The enzyme was precipitated from the extract by ammonium sulfate, dialyzed, chromatographed on Sephadex G 100 column, and then purified by polyacrylamide gel electrophoresis Its fibrinolytic activity was assessed with fibrin plate method Results The purified enzyme showed an isoelectric point (PI) around 4 5 as tested by gel isoelectric focusing It consisted of two polypeptide chains with molecular weights around 33 000 u and 14 400 u, respectively Conclusion This was a novel fibrinolytic enzyme discovered from P aibuhitensis for the first time