Hypochlorite-Induced Oxidative Modification of Fibrinogen

Oxidation of fibrinogen with hypochlorite inhibited the fibrin network self-assembly even at the lowest concentration of the oxidant. The analysis of the results of protein electrophoresis at this hypochlorite concentration showed the absence of fragmentation of the protein and covalent cross-linkin...

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Published inDoklady. Biochemistry and biophysics Vol. 484; no. 1; pp. 37 - 41
Main Authors Yurina, L. V., Vasilyeva, A. D., Bugrova, A. E., Indeykina, M. I., Kononikhin, A. S., Nikolaev, E. N., Rosenfeld, M. A.
Format Journal Article
LanguageEnglish
Published Moscow Pleiades Publishing 01.05.2019
Springer Nature B.V
Subjects
Amino acids
Biochemistry
Biological and Medical Physics
Biomedical and Life Sciences
Biophysics
Fibrin
Fibrinogen
Life Sciences
Mass spectroscopy
Molecular Biology
Oxidation
Self-assembly
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Summary:Oxidation of fibrinogen with hypochlorite inhibited the fibrin network self-assembly even at the lowest concentration of the oxidant. The analysis of the results of protein electrophoresis at this hypochlorite concentration showed the absence of fragmentation of the protein and covalent cross-linking of its chains. The study of the areas responsible for the conversion of fibrinogen into fibrin by mass spectrometry showed that they are not subject to oxidative damage. However, we identified oxidized amino acid residues, which could affect the protofibril aggregation.
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ISSN:1607-6729
1608-3091
1608-3091
DOI:10.1134/S1607672919010101