The Structural–Functional Damage of Fibrinogen Oxidized by Hydrogen Peroxide

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...

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Veröffentlicht in:	Doklady. Biochemistry and biophysics 2020-05, Vol.492 (1), p.130-134
Hauptverfasser:	Yurina, L. V., Vasilyeva, A. D., Kononenko, V. L., Bugrova, A. E., Indeykina, M. I., Kononikhin, A. S., Nikolaev, E. N., Rosenfeld, M. A.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino acid sequence Biochemistry Biological and Medical Physics Biomedical and Life Sciences Biophysics Factor XIIIa - metabolism Fibrin Fibrin - chemistry Fibrinogen Fibrinogen - chemistry Fibrinogen - drug effects Fibrinogen - metabolism Fibrinolysin - metabolism Humans Hydrogen peroxide Hydrogen Peroxide - pharmacology Life Sciences Molecular Biology Oxidants - pharmacology Oxidation Oxidation-Reduction Plasmin Structure-Activity Relationship Structure-function relationships
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Zusammenfassung:	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.
ISSN:	1607-6729 1608-3091
DOI:	10.1134/S1607672920020167