纤维蛋白原西雅图II型：一种伴有精氨酸（Aα16）置换的先天性异常纤维蛋白原血症。

Fibrinogen Seattle II: congenital dysfibrinogenemia with an Arg (A alpha 16)----his substitution.

作者信息

Ebert R F, Schreiler W E, Bell W R

出版信息

Thromb Res. 1986 Jul 1;43(1):7-13. doi: 10.1016/0049-3848(86)90040-x.

Abstract

Incubation of fibrinogen Seattle II with thrombin (17 mu/ml) resulted in the release of two forms of fibrinopeptide A (FpA) which were resolved by high-performance liquid chromatography. Amino acid analysis disclosed that the abnormal FpA contained histidine in place of arginine. At lower, approximately physiologic thrombin concentrations only half the normal amount of FpA was released, and fibrinopeptide B (FpB) release was delayed. The effect of this substitution on the time course of fibrinopeptide release is consistent with conclusions drawn from other studies on the kinetics of fibrinopeptide release, viz., that prior removal of FpA is not required before FpB hydrolysis by thrombin, and that optimal rates of FpB release occur after formation of fibrin I polymer.

摘要

将纤维蛋白原西雅图II与凝血酶（17 mu/ml）一起温育，导致释放出两种形式的纤维蛋白肽A（FpA），它们通过高效液相色谱法得以分离。氨基酸分析表明，异常的FpA含有组氨酸而非精氨酸。在较低的、大约为生理浓度的凝血酶条件下，仅释放出正常量一半的FpA，并且纤维蛋白肽B（FpB）的释放延迟。这种取代对纤维蛋白肽释放时间进程的影响与其他关于纤维蛋白肽释放动力学研究得出的结论一致，即凝血酶水解FpB之前无需预先去除FpA，并且FpB释放的最佳速率在纤维蛋白I聚合物形成之后出现。