The Structural–Functional Damage of Fibrinogen Oxidized by Hydrogen Peroxide

L. V. Yurina, A. D. Vasilyeva, V. L. Kononenko, A. E. Bugrova, M. I. Indeykina, A. S. Kononikhin, E. N. Nikolaev, M. A. Rosenfeld

    Research output: Contribution to journalArticlepeer-review

    5 Citations (Scopus)


    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.

    Original languageEnglish
    Pages (from-to)130-134
    Number of pages5
    JournalDoklady Biochemistry and Biophysics
    Issue number1
    Publication statusPublished - 1 May 2020


    • fibrin gel
    • fibrinogen
    • HPLC-MS/MS
    • microrheology
    • oxidation
    • oxidation sites
    • PAGE


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