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Updated: Dec 15, 2025

Experimental and Imaging Techniques for Examining Fibrin Clot Structures in Normal and Diseased States
Published on: April 1, 2015
The Structural-Functional Damage of Fibrinogen Oxidized by Hydrogen Peroxide
L V Yurina1,2,3,4, A D Vasilyeva5, V L Kononenko5
1Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, Russia. lyu.yurina@gmail.com.
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.
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