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锌抑制纤维蛋白原激活物释放并增加纤维蛋白浊度。

Zinc inhibits FPA release and increases fibrin turbidity.

作者信息

Marx G, Hopmeier P

出版信息

Am J Hematol. 1986 Aug;22(4):347-53. doi: 10.1002/ajh.2830220403.

Abstract

Physiologic concentrations of Zn(II) (4-40 microM) can increase the rate of thrombin-induced fibrin clot formation (decreased clotting time, CT) and increase the turbidity of the fibrin gel. Both the initial and ultimate turbidity (AbS 600 nm) of fibrin gels are increased in the presence of Zn(II). Two techniques were used to elaborate the mechanisms of Zn+2 procoagulant effect. Analytical ultracentrifugation indicates that Zn(II) does not induce the formation of fibrinogen multimers. Radioimmunoassay for FPA indicates that thrombin activation of fibrinogen is decreased by Zn(II), with 50% inhibition of FPA release observed at 35 microM Zn(II). These experiments indicate that the critical feature of Zn(II) procoagulant effect is not due to the induction of fibrinogen proteolysis by thrombin, which is actually decreased. Rather, it appears that Zn(II) accelerates the polymerization step of fibrin assembly and concomitantly modifies fibrin gel structure.

摘要

生理浓度的锌离子(Zn(II),4 - 40微摩尔)可加快凝血酶诱导的纤维蛋白凝块形成速率(凝血时间[CT]缩短),并增加纤维蛋白凝胶的浊度。在锌离子存在的情况下,纤维蛋白凝胶的初始浊度和最终浊度(600纳米处的吸光度)均会增加。采用了两种技术来阐明锌离子促凝作用的机制。分析超速离心表明,锌离子不会诱导纤维蛋白原多聚体的形成。纤维蛋白肽A(FPA)的放射免疫分析表明,锌离子会降低凝血酶对纤维蛋白原的激活作用,在35微摩尔锌离子时观察到FPA释放受到50%的抑制。这些实验表明,锌离子促凝作用的关键特征并非由于凝血酶诱导的纤维蛋白原蛋白水解作用,而实际上这种作用是减弱的。相反,似乎锌离子加速了纤维蛋白组装的聚合步骤,并同时改变了纤维蛋白凝胶结构。

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