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Effect of Hypochlorite- and Peroxide-Induced Oxidation of Fibrinogen on the Fibrin Structure
Doklady Biochemistry and Biophysics ( IF 0.8 ) Pub Date : 2021-08-23 , DOI: 10.1134/s1607672921040189
L V Yurina 1 , A D Vasilyeva 1 , L A Vasserman 1 , N A Podoplelova 2, 3 , M A Panteleev 2, 3 , M A Rosenfeld 1
Affiliation  

Abstract

Using the methods of dynamic and elastic light scattering and confocal laser scanning microscopy, the damage in the spatial fibrin structure during peroxide- and hypochlorite-induced oxidation of fibrinogen was studied. Peroxide had a weak effect on the structural organization of fibrin, whereas hypochlorite caused the formation of abnormal fibrin with reduced individual fiber diameter and decreased porosity. Measurements of the size distributions of the native and oxidized fibrinogen revealed a decrease in the hydrodynamic size of the oxidized fibrinogen molecule with an increase in the concentration of oxidizers. These results indicate that the hydrophobicity of fibrinogen surface increased and its colloidal stability decreased. The possible role of oxidative sites in the assembly of structurally abnormal fibrin is analyzed.



中文翻译:


次氯酸盐和过氧化物诱导的纤维蛋白原氧化对纤维蛋白结构的影响


 抽象的


采用动态弹性光散射和共焦激光扫描显微镜方法,研究了过氧化物和次氯酸盐诱导的纤维蛋白原氧化过程中空间纤维蛋白结构的损伤。过氧化物对纤维蛋白的结构组织影响较弱,而次氯酸盐则导致异常纤维蛋白的形成,使单纤维直径减小,孔隙率降低。对天然纤维蛋白原和氧化纤维蛋白原的尺寸分布的测量表明,随着氧化剂浓度的增加,氧化纤维蛋白原分子的流体动力学尺寸减小。这些结果表明纤维蛋白原表面的疏水性增加并且其胶体稳定性降低。分析了氧化位点在结构异常纤维蛋白组装中的可能作用。

更新日期:2021-08-24
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