[Polymorphism of fibrin equilibrium oligomers in the presence of fragment D].
The methods of viscosimetry, the Rayleigh light-scattering and analytical ultracentrifugation were applied to study the physicochemical mechanism of the effect of fragment D on the structure of fibrin equilibrium oligomers. Using the values of intrinsic viscosity, weight average molecular masses and mass/length ratio it was shown that when producing an antipolymerization effect the fragment D retains the three-dimensional organization of fibrin polymers, i.e. rigid rod-like single- and double-stranded protofibrillas. The paper has proved that along with the traditional mechanism of inhibiting self-assembly of of the double-stranded structure due to the competition of fragment D with fibrin monomer for central domain E there is an alternative attributed to its attachment to a peripheral region of the fibrin monomer. The second mechanism is the only one which occurs in the region of single-stranded pseudoprotofibrillas existence. The role of alpha C-domains in protein-protein interactions is also discussed.
Gershkovich
K B
KB
Rozenfel'd
M A
MA
D000818:Animals; D002417:Cattle; D005337:Fibrin / Q000032:analysis*; D005338:Fibrin Fibrinogen Degradation Products / Q000032:analysis*; D008027:Light; D008970:Molecular Weight; D011487:Protein Conformation; D012542:Scattering, Radiation; D014783:Viscosity
D005338:Fibrin Fibrinogen Degradation Products; C015214:fibrinogen D fragment; D005337:Fibrin
Polimorfizm ravnovesnykh oligomerov fibrina v prisutstvii fragmenta D.