Nidialkova N A, Matseliukh O V, Varbanets' L D
Mikrobiol Z. 2012 Sep-Oct;74(5):9-15.
Fibrinolytic peptidase of Bacillus thuringiensis IMV B-7324 was isolated by ammonium sulfate fractionation, gel-filtration and ion exchange chromatography on TSK-gels--Toyopearl HW-55 and DEAE 650 (M). Fibrinolytic activity of the purified enzyme was 87.9 U/mg of protein that was 19.9 times higher compared with the supernatant cultural liquid, the yield on its activity reached 31%. The gel-filtration on Sepharose 6B and by SDS-PAGE electrophoresis demonstrated the homogeneity of the purified fibrinolytic peptidase, which molecular weight was approximately 24 kDa.
通过硫酸铵分级沉淀、凝胶过滤以及在TSK凝胶（Toyopearl HW - 55和DEAE 650 (M)）上进行离子交换色谱法，从苏云金芽孢杆菌IMV B - 7324中分离出纤溶肽酶。纯化酶的纤溶活性为87.9 U/mg蛋白质，比上清培养液高19.9倍，其活性产率达到31%。在琼脂糖凝胶6B上进行的凝胶过滤和SDS - PAGE电泳表明纯化的纤溶肽酶具有均一性，其分子量约为24 kDa。
