The Mechanism of Cross-Linking of Fibrinogen and Its Early Structural Homolog—XFragment.

Autor: Rozenfel'd, M., Kostanova, E., Vasil'eva, M., Leonova, V.
Zdroj: Biology Bulletin; May2001, Vol. 28 Issue 3, p238-243, 6p
Abstrakt: We studied the mechanism of the cross-linking of fibrinogen, as well as its closest structural homolog Xfragment, under the influence of a fibronectin-stabilizing factor (factor XIIIa). The data on elastic and dynamic light scattering indicate the formation of single-stranded polymers without any structural rigidity that acquire a ramified and compact structure upon reaching critical mass. The values of coefficients of translational diffusion, mean-mass molecular weight, averaged scattering factor, and the accumulation of γ-dimers indicate that preincubating of fibrinogen and fragment Xsolutions significantly accelerates the enzymatic formation of a covalently bound macromolecular protein complex. We propose that enzymatic cross-linking proceeds only with the gradual accumulation of structurally imperfect molecules of fibrinogen and fragment Xthat are prone to intermolecular D–Dend-to-end contacts. [ABSTRACT FROM AUTHOR]
Databáze: Complementary Index
Externí odkaz: