蚓激酶活性成分的分离纯化

目的本实验采用色谱分离的方法从赤子爱胜蚓（EiseniaFoelide）中分离纯化出一种纯度达到95％以上的蚯蚓纤溶酶。方法采用匀浆抽提、热变性、超滤、色谱分离、SDS—PAcE和高效液相色谱法等技术对蚓激酶进行分离纯化及鉴定，并用纤维平板法测定其活性。结果通过一系列纯化步骤所得的蚓激酶比活120000u／mg，经sDs—PAGE分析得一条带，相对分子量为28000Da；高效液相色谱分析其纯度达95％以上。结论本实验从蚯蚓中分离纯化出一种高活性、高纯度的蚓激酶。

Separation and Purification of lumbrokinase

Objective To obtain a lumbrokinase with a purity over 95% from eisenia fetida earthworm by chromatography. Methods Lumbrokinase was purified through extraction, thermal denaturation, uhrafihration, and hromategraphy from Eisenia foelide and identified by SDS-PAGE and HPLC. The activity was detected by the firbrin plate method. Results The specific activity of the obtained lumbrokinase was 120 000 U/rag. One band of 28 000Da was obtained by SDS-PAGE and HPLC showed that its purify was higher than 95%. Conclusions A single component of protein with high thrombolysis activity and high purify was separated and purified from Eisenia Foelide.