摘要
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 2 2～ 34ku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、ChromozymUK和ChromozymPL为底物测定 ,7的纤溶酶活性最高 .
The earthworm fibrinolytic enzymes (EFE) were separated by affinity chromatography using soybean trypsin inhibitor as a matrix. The enzymes were further separated and purified into 12 components after DEAE-32 chromatography and preparative electrophoresis. The pi of these components gradually decreased from pH 4.0 according to electrophoresis mobility from higher to lower on PAGE. The molecular weights were in the range of 22 similar to 34 ku. 6.5 and 7 were glycoproteins proved by staining with the shiff reagent and thymol/sulfuric acid. The fibrinolytic activity of 7 was highest as determined using chromzym UK and chromzym PL as specific substrates.
出处
《生物化学与生物物理进展》
SCIE
CAS
CSCD
北大核心
2001年第2期218-221,共4页
Progress In Biochemistry and Biophysics
关键词
蚯蚓纤溶酶
组分
分离
纯化
酶活
earthworm
fibrinolytic enzyme
component
separation
purification
fibrinolytic activity
