Subunit Structure of Human Fibrinogen, Soluble Fibrin, and Cross-Linked Insoluble Fibrin*
AUTOR(ES)
McKee, Patrick A.
RESUMO
The three unique polypeptide chains of human fibrinogen differ significantly in molecular weight. Cross-linkage of fibrin by fibrin-stabilizing factor results in the rapid formation of cross-links between γ-chains and a slower formation of cross-links between α-chains. β-Chains are not involved directly in the cross-linking of fibrin. Reduced, cross-linked fibrin contains uncross-linked β-chains, dimers of γ-chain, and higher polymers of α-chain. Although it is uncertain whether the γ-γ dimers are formed by chains in different molecules of fibrin, the polymers of α-chain in fibrin can only be accounted for by cross-linkage of α-chains in different molecules. The nature of cross-linkage among the subunits in fibrin can account well for the three-dimensional, covalent structure of cross-linked, insoluble fibrin.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=283112Documentos Relacionados
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