| Literature DB >> 26518549 |
M A Rosenfeld1, V B Leonova2, A V Bychkova2, E A Kostanova2, M I Biryukova2.
Abstract
The crosslinking of fibrin γ-polypeptide chains under the influence of the plasma fibrin-stabilizing factor (FXIIIa), which causes their conversion to γ-γ dimers, is the major enzyme reaction of covalent fibrin stabilization. We studied the self-assembly of soluble cross-linked fibrin oligomers. The results of analytical ultracentrifugation as well as elastic and dynamic light scattering showed that the double-stranded fibrin oligomers formed under the influence of moderate concentrations of urea are cross-linked only due to formation of γ-γ dimers, which can dissociate into single-stranded structure when the concentration of urea increases. This fact proves that γ-γ dimers are formed in the end-to-end manner.Entities:
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Year: 2015 PMID: 26518549 DOI: 10.1134/S1607672915050051
Source DB: PubMed Journal: Dokl Biochem Biophys ISSN: 1607-6729 Impact factor: 0.788