鼠肾纤维蛋白溶酶原激活酶的纯化和部分鉴定

PURIFICATION AND PARTIAL CHARACTERIZATION OF A TISSUE PLASMINOGEN ACTIVATOR FROM MOUSE KIDNEYS

采用肝素—Sepharose亲和层析和凝胶过滤自鼠肾提取纤维蛋白溶酶原激活酶,产率5.1×10^(-5)％。在还原和非还原状态下SDS—聚丙烯酰胺凝胶电泳及电泳酶谱分析均呈单一区带,证实产物仍保持单链状态。测得其分子量为70000。纤维平板试验和无纤维蛋白溶酶原纤维平板试验证实其活性依赖于纤维蛋白溶酶原。

This paper described a method for the isolation of tissue type plasminogen activator(t-PA) from mouse kidneys using adsorption to heparin-Sepharose as the essential step. 0.083 mg of the purified enzyme was abtained from 164.3g fresh wet tissue. It has been shown that the final product consists of one polypeptide chain keeping the native form with the molecular weight of 70000. The product gave a single band both in SDS-polyacrylamide gels (in the presence or absence of the reducing agent) or in electrophoretic zymogram.