[Mechanism of cross-linking of fibrinogen and its early structural homolog fragment X].
We studied the mechanism of the cross-linking of fibrinogen as well as its closest structural homolog X fragment 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 gamma-dimers indicate that preincubation of fibrinogen and fragment X solutions 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 X that are prone to intermolecular D-D end-to-end contacts.
Rozenfel'd
M A
MA
Institute of Biochemical Physics, Russian Academy of Sciences, ul. Kosygina 4, Moscow, 117977 Russia.
Kostanova
E A
EA
Vasil'eva
M V
MV
Leonova
V B
VB
D000818:Animals; D002417:Cattle; D003432:Cross-Linking Reagents / Q000737:chemistry*; D004586:Electrophoresis; D005176:Factor XIII / Q000737:chemistry*; D005338:Fibrin Fibrinogen Degradation Products / Q000737:chemistry*; D005340:Fibrinogen / Q000737:chemistry*; D008027:Light; D008970:Molecular Weight; D012542:Scattering, Radiation
D003432:Cross-Linking Reagents; D005338:Fibrin Fibrinogen Degradation Products; C030568:fibrinogen fragment X; D005340:Fibrinogen; D005176:Factor XIII