[alphaC domains of fibrinogen molecules as the structures accelerating fibrin assembly].
Preparation of monomeric fibrin lacking intact alpha C-domains (monomeric X1-fragment), but fully clottable, is described. The assembly process of both monomeric fibrin and monomeric X1-fragment has been studied by electron microscopy and light scattering methods. It was shown that both proteins form similar fibrils with characteristic cross-banding. Upon dilution a sharp elevation of the differences between the assembly rates of monomeric X1-fragment and monomeric fibrin was revealed. The results obtained show that alpha C-domains take part in fibrin clot formation not as structural components but as the factor accelerating the ordered assembly of complex fibrin structure. The possible mechanism of alpha C-domains participation in fibrin clot formation are regarded.
Medved'
L V
LV
Gorkun
O V
OV
Maniakov
V F
VF
Belitser
V A
VA
D000818:Animals; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D005337:Fibrin / Q000032:analysis*; D005338:Fibrin Fibrinogen Degradation Products / Q000032:analysis*; D005340:Fibrinogen / Q000032:analysis*; D006868:Hydrolysis; D066298:In Vitro Techniques; D008958:Models, Molecular; D011487:Protein Conformation
D005338:Fibrin Fibrinogen Degradation Products; C030568:fibrinogen fragment X; D005337:Fibrin; D005340:Fibrinogen
alphaC-domeny molekuly fibrinogena kak struktury, uskoriaiushchie samosborku fibrina.