[The effect of fragment D on the aggregation of fibrinogen molecules in solution].
The mechanism of fibrinogen aggregation in the presence of fragment D has been studied. The values of translational diffusion coefficients, specific viscosity, average molecular masses, and Zimm factor of light scattering indicate that fragment D accelerated assembly of fibrinogen molecules that form flexible polymeric chains with tail-to-tail association due to spontaneous structural modification of COOH-terminal regions. Electrophoresis did not reveal the presence of fragment D in polymer fraction of non-reduced samples. The data obtained allowed to conclude that at initial stages fragment D forms unstable complexes with structurally modified fibrinogen molecules. These complexes serve as intermediates in the multistep process of assembly of supermolecular protein complex.
Rozenfel'd
M A
MA
Vasil'eva
M V
MV
Gershkovich
K B
KB
D001797:Blood Protein Electrophoresis; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004347:Drug Interactions; D004591:Electrophoresis, Polyacrylamide Gel; D005338:Fibrin Fibrinogen Degradation Products / Q000032:analysis / Q000302:isolation & purification / Q000494:pharmacology*; D005340:Fibrinogen / Q000032:analysis / Q000187:drug effects* / Q000302:isolation & purification; D006801:Humans; D066298:In Vitro Techniques; D012996:Solutions
D005338:Fibrin Fibrinogen Degradation Products; D012996:Solutions; C015214:fibrinogen D fragment; D005340:Fibrinogen
Vliianie fragmenta D na agregatsiiu molekul fibrinogena v rastvore.