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Dokl Biochem Biophys ; 466: 28-31, 2016.
Article in English | MEDLINE | ID: mdl-27025482

ABSTRACT

The effect on ozone-induced oxidation on the self-assembly of fibrin in the presence of fibrin-stabilizing factor FXIIIa of soluble cross-linked fibrin oligomers was studied in a medium containing moderate urea concentrations. It is established that fibrin oligomers were formed by the protofibrils cross-linked through γ-γ dimers and the fibrils additionally cross-linked by through α-polymers. The oxidation promoted both the accumulation of greater amounts of γ-γ dimers and the formation of protofibrils, fibrils, and their dissociation products emerging with increasing urea concentrations, which have a high molecular weight. It is concluded that the oxidation enhances the axial interactions between D-regions of fibrin molecules.


Subject(s)
Fibrin/chemistry , Protein Multimerization , Factor XIII/chemistry , Factor XIII/metabolism , Fibrin/metabolism , Humans , Oxidation-Reduction , Protein Binding , Urea/chemistry
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