title: Soluble fibrin-fibrinogen complexes as intermediates in fibrin gel formation.
abstract: Oligomer formation in fibrinogen solutions following addition of thrombin was studied by addition of thrombin inhibitor at various times subsequent to thrombin, followed by size-exclusion chromatography (SEC) on a high-performance SEC column capable of resolving species of molecular weights less than or equal to 10(6). Peaks corresponding to species with 1, 2, 3, and 4 or more times the molecular weight of fibrinogen were detected and quantified via nonlinear least-squares curve-fitting procedures. The evolution of each of these peaks with time is well accounted for by a kinetic model in which the predominant component of each oligomeric molecular weight species is a linear complex of fibrinogen and fibrin. The observed predominance of trimeric over dimeric oligomers even at short times suggests that the thrombin-catalyzed release of the two A fibrinopeptides from a single molecule of fibrinogen is highly cooperative.
mesh_terms: D000818:Animals; D002417:Cattle; D002850:Chromatography, Gel; D005337:Fibrin / Q000378:metabolism*; D005340:Fibrinogen / Q000378:metabolism*; D005782:Gels; D006801:Humans; D007700:Kinetics; D046911:Macromolecular Substances; D008433:Mathematics; D008970:Molecular Weight; D013917:Thrombin / Q000378:metabolism
chemical_list: D005782:Gels; D046911:Macromolecular Substances; D005337:Fibrin; D005340:Fibrinogen; D013917:Thrombin