Longitudinal orientation of cross-linked polypeptide γ chains in fibrin fibrils

Rosenfeld, M.; Leonova, V.; Bychkova, A.; Kostanova, E.; Biryukova, M.
September 2015
Doklady Biochemistry & Biophysics;Sep2015, Vol. 464 Issue 1, p286
Academic Journal
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.


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