抗凝血酶“维琴察”的纯化：一种具有正常肝素亲和力但对凝血酶反应性受损的分子。

Purification of antithrombin 'Vicenza': a molecule with normal heparin affinity and impaired reactivity to thrombin.

作者信息

Finazzi G, Tran T H, Barbui T, Duckert F

出版信息

Br J Haematol. 1985 Feb;59(2):259-63. doi: 10.1111/j.1365-2141.1985.tb02992.x.

DOI:10.1111/j.1365-2141.1985.tb02992.x

Abstract

Antithrombin III (AT) 'Vicenza', a previously described dysfunctional AT associated with familial thrombosis, has been isolated by heparin affinity chromatography. The purified molecule has been investigated by SDS-polyacrylamide gel electrophoresis and crossed immunoelectrophoresis after incubation with different amounts of thrombin. A normal affinity for heparin has been demonstrated. However, evidence is produced that AT 'Vicenza' poorly inhibits thrombin. Present data suggest that AT 'Vicenza' consists of a population of two molecules, half of which does not form a complex with thrombin however and loses its heparin affinity upon thrombin treatment.

摘要

抗凝血酶III（AT）“维琴察”是一种先前描述的与家族性血栓形成相关的功能失调的AT，已通过肝素亲和层析法分离出来。纯化后的分子经十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（SDS-聚丙烯酰胺凝胶电泳）和与不同量凝血酶孵育后的交叉免疫电泳分析。已证实其对肝素有正常亲和力。然而，有证据表明AT“维琴察”对凝血酶的抑制作用较弱。目前的数据表明，AT“维琴察”由两种分子组成，其中一半分子不能与凝血酶形成复合物，并且在凝血酶处理后失去其肝素亲和力。