Nanninga L B, Guest M M
Thromb Haemost. 1979 Oct 31;42(3):855-63.
A method is described for the purification of antiactivator from bovine euglobulin-free serum by means of gelfiltration and ion exchange chromatography. The purified antiactivator has no antifibrinolytic activity. It has a molecular weight of about 115,000 and it appears to be a gamma globulin. The dissociation constant of its complex with urokinase is 1.6 x 10(-9) M and the maximum urokinase binding is close to 2000 CTA units per mg. Its concentration in bovine serum is 0.37%. Flufenamate displaces urokinase from the antiactivator at very low concentrations, about 10(-4) M. Cysteine restores its activity if lost by standing. Also an antifibrinolysin fraction is obtained free of antiactivator activity.
本文描述了一种通过凝胶过滤和离子交换色谱法从无优球蛋白的牛血清中纯化抗激活剂的方法。纯化后的抗激活剂没有抗纤溶活性。它的分子量约为115,000，似乎是一种γ球蛋白。它与尿激酶形成的复合物的解离常数为1.6×10⁻⁹M，最大尿激酶结合量接近每毫克2000个CTA单位。其在牛血清中的浓度为0.37%。氟灭酸在极低浓度（约10⁻⁴M）时就能从抗激活剂上置换出尿激酶。如果因放置而失去活性，半胱氨酸可恢复其活性。此外，还获得了无抗激活剂活性的抗纤溶酶组分。
