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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1970 Jul;66(3):738–744. doi: 10.1073/pnas.66.3.738

Subunit Structure of Human Fibrinogen, Soluble Fibrin, and Cross-Linked Insoluble Fibrin*

Patrick A McKee 1,2, Patrick Mattock 1,2, Robert L Hill 1,2,†
PMCID: PMC283112  PMID: 5269236

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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