蚯蚓纤溶酶组分的分离纯化和分析

通过以大豆胰蛋白酶抑制剂为配基的亲和层析，从蚯蚓（大平二号, 即赤子爱胜蚓）纯化出的纤溶酶是一组非均一的纤维蛋白水解酶.经DEAE-纤维素离子交换和制备电泳进一步分离纯化，得到12个单一组分. 这些组分的等电点(pI)按照它们在聚丙烯酰胺凝胶电泳(PAGE)图谱上的顺序从4.0开始依次降低; SDS-PAGE证明, 除3、4外，其余组分均只含一种多肽链，分子质量在22～34 ku之间；用shiff试剂和酚-硫酸染色, 显示1、2、6.5和7是糖蛋白，其中7的糖含量最高; 以BAEE、Chromozym UK和Chromozym PL为底物测定，7的纤溶酶活性最高.

Separation, Purification and Analysis of the Components of Earthworm Fibrinolytic Enzymes

The earthworm fibrinolytic enzymes (EFE) were separated by affinity ch romatography using soybean trypsin inhibitor as a matrix. The enzymes were furth er separated and purified into 12 components after DEAE-32 chromatography and p reparative electrophoresis. The pI of these components gradually decreased f rom pH 4.0 according to electrophoresis mobility from higher to lower on PAGE. The molecular weights were in the range of 22～34 ku. 6.5 and 7 w ere glycoproteins proved by staining with the shiff reagent and thymol/sulfuric acid. The fibrinolytic activity of 7 was highest as determined usi ng chromzym UK and chromzym PL as specific substrates.