目的 :以枯草杆菌HL 986发酵液为原料 ,对枯草杆菌溶栓酶的分离纯化技术进行研究。方法 :采用磷酸钙吸附沉淀除去部分色素和杂蛋白 ,经超滤脱盐、CM 5 2离子交换分离、丙酮沉淀和SephadexG 75凝胶过滤处理 ,得到具有溶栓活性的酶。结果 :得到的溶栓酶在SDS PAGE上为单一谱带 ,其分子量约为 2 7kD ,比活为980 0U/mg,活性得率为 6 3.8%。结论 :以较高的得率获得了高纯度的枯草杆菌溶栓酶。 OBJECTIVE: To study the separation and purification of Bacillus subtilis thrombolytic enzyme by using Bacillus subtilis HL 986 fermentation broth as raw material. METHODS: Part of pigment and hybrid protein were removed by calcium phosphate precipitation. After ultrafiltration desalination, CM 5 2 ion exchange separation, acetone precipitation and Sephadex G 75 gel filtration, the thrombolytic activity of the enzyme was obtained. Results: The obtained thrombolytic enzyme had a single band on SDS PAGE. The molecular weight was about 27kD, the specific activity was 980 0U / mg and the activity yield was 6 3.8%. Conclusion: High purity Bacillus subtilis thrombolytic enzyme was obtained with high yield.