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凝血因子XIII在正常及病理状态下对纤维蛋白结构的作用机制。

Mechanism of the action of factor XIII on the structure of fibrin in the normal and pathological states.

作者信息

Kleimenov A N, Rozenfel'd M A, Piruzyan L A, Titova M I, Shimkevich L L

出版信息

Biol Bull Acad Sci USSR. 1978 Sep-Oct;5(5):610-4.

PMID:754811
Abstract

The work discusses the influence of factor XIII on the molecular structure of fibrin and its properties under normal conditions and in certain forms of coagulopathies. It was shown that the reaction of stabilization is accompanied by an exothermic effect, the thermal effect of which on donor blood plasma is 15.5 kcal/mole. It was also established that the enrichment of blood plasma with fibrinogen leads to an increase in the thermal effect, which is due to the influence of the density of the terminal and lateral bonds in the fibrin molecule and the process of its covalent cross-linking. An examination of groups of patients structure of fibrin and its physiological properties, on account of a change in the number of peptide bonds formed. On the basis of the results obtained, a new energy test for the determination of the fibrin-stabilizing factor is suggested.

摘要

这项工作讨论了因子 XIII 在正常条件下以及某些形式的凝血病中对纤维蛋白分子结构及其特性的影响。结果表明,稳定反应伴随着放热效应,其对供血者血浆的热效应为 15.5 千卡/摩尔。还确定了血浆中纤维蛋白原的富集导致热效应增加,这是由于纤维蛋白分子中末端和侧链键的密度及其共价交联过程的影响。根据形成的肽键数量的变化,对患者组的纤维蛋白结构及其生理特性进行了检查。基于所得结果,提出了一种用于测定纤维蛋白稳定因子的新能量测试方法。

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