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纤维蛋白原与固定化去氨甲酰基纤维蛋白的交联

Crosslinking of fibrinogen to immobilized DesAA-fibrin.

作者信息

Selmayr E, Thiel W, Müller-Berghaus G

出版信息

Thromb Res. 1985 Aug 15;39(4):459-65. doi: 10.1016/0049-3848(85)90169-0.

Abstract

DesAA-fibrin Sepharose was produced by treating fibrinogen-Sepharose with batroxobin. DesAA-fibrin Sepharose was mixed with different concentrations of fibrinogen and at different ratios, and incubated with preactivated FXIII. After 2 hours at 37 degrees C, the Sepharose beads were separated by centrifugation and non-crosslinked fibrinogen was removed by twice times washing with guanidinium chloride, pH 4.1. Under these experimental conditions specific crosslinking of fibrinogen to immobilized desAA-fibrin by FXIIIa was found. These results support the concept of a specific interaction between fibrinogen and fibrin involving polymerization which enables FXIIIa to crosslink fibrin to fibrinogen being in an half-staggered overlap position but not in DD-long contact.

摘要

去Aα纤维蛋白琼脂糖凝胶是通过用巴曲酶处理纤维蛋白原琼脂糖凝胶制备而成。将去Aα纤维蛋白琼脂糖凝胶与不同浓度的纤维蛋白原以不同比例混合,并与预激活的因子XIII(FXIII)一起孵育。在37℃下孵育2小时后,通过离心分离琼脂糖珠,并通过用pH 4.1的氯化胍洗涤两次去除未交联的纤维蛋白原。在这些实验条件下,发现因子XIIIa(FXIIIa)能使纤维蛋白原与固定化的去Aα纤维蛋白发生特异性交联。这些结果支持了纤维蛋白原与纤维蛋白之间存在特异性相互作用的概念,这种相互作用涉及聚合反应,使得FXIIIa能够将纤维蛋白交联到处于半交错重叠位置而非DD长接触位置的纤维蛋白原上。

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