论文部分内容阅读
尿激酶前体是与尿激酶具有共同抗原性的一种新的纤溶酶原激活物。我们从人胎肾细胞条件培养液中提纯该物质。首先用抗UKIgG-Sepharose亲和层析得到尿激酶抗原相关蛋白,然后利用苯甲脒-Sepharose柱去除尿激酶获纯化的尿激酶前体。纯化倍数达930倍,得率为18%,所得尿激酶前体为单肽链结构蛋白质,分子量55kD,比活(11389IU/mg)低于尿激酶,二异丙基氟磷酸酯(DFP)不能抑制其活性。体外_~(125)I-血凝块溶解试验表明尿激酶前体可特异地诱导血凝块溶解,对血浆纤溶系统无明显激活作用,血凝块溶解的时间曲线呈特征性“S”型。所得尿激酶前体是一种新的有别于尿激酶的纤溶酶原激活物。
Urokinase precursors are a novel plasminogen activator that shares antigenic properties with urokinase. We purified this material from human fetal kidney cell conditioned medium. Urokinase antigen-related proteins were first obtained by affinity chromatography with anti-UKIgG-Sepharose and then purified by urokinase using a benzamidine-Sepharose column. The purification factor was 930 times, and the yield was 18%. The obtained urokinase precursor was a single peptide chain structure protein with a molecular weight of 55 kD, lower specific activity (11389 IU / mg) than urokinase and no diisopropyl fluorophosphate (DFP) Inhibit its activity. In vitro 125I-clot lysis assay showed that urokinase precursor can specifically induce the clot lysis without obvious activation of the fibrinolytic system, the time curve of lysis of blood clot is characteristic “S” type. The resulting urokinase precursor is a novel plasminogen activator that is distinct from urokinase.