Abstract

The effect of peroxide-induced oxidation of fibrinogen on modification of its primary structure and functional properties was investigated. The oxidation sites were shown to be Met, Trp, and His residues. Using the DLS method, it was found that the oxidative modification of fibrinogen results in the change of microrheological characteristics of fibrin network. The fibrinogen oxidation diminishes its tolerance to plasmin hydrolysis and deteriorates the factor XIIIa ability to stabilize the fibrin gel.

中文翻译：

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纤维蛋白原的结构功能损伤被过氧化氢氧化。

摘要

研究了过氧化物诱导的纤维蛋白原氧化对其一级结构和功能特性的影响。氧化位点显示为Met，Trp和His残基。使用DLS方法，发现纤维蛋白原的氧化修饰导致纤维蛋白网络的微流变特性的改变。纤维蛋白原的氧化削弱了其对纤溶酶水解的耐受性，并破坏了因子XIIIa稳定纤维蛋白凝胶的能力。