Abstract
Fibrinogen (1) is a dimeric, symmetrical molecule with the overall structure (Aα, Bβ, γ)2. When fibrinogen is converted into fibrin by the action of thrombin two moles of each fibrinopeptide A and B are finally released. Hereby four N-terminal polymerization sites are revealed in each molecule and these can then interact with four pre-existing C-terminal polymerization sites so that fibrin oligomers and polymers are formed. It is well established that A-peptides are removed from fibrinogen before B-peptides and that A-peptide release alone is sufficient for clotting to occur. The two fibrin types formed have the structures [(α, β, γ)2]n and [(α, Bβ, γ)2]n respectively.
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© 1990 Springer Science+Business Media New York
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Henschen, A. (1990). On the Identity of Fibrin(ogen) Oligomers Appearing during Fibrin Polymerization. In: Liu, C.Y., Chien, S. (eds) Fibrinogen, Thrombosis, Coagulation, and Fibrinolysis. Advances in Experimental Medicine and Biology, vol 281. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-3806-6_4
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DOI: https://doi.org/10.1007/978-1-4615-3806-6_4
Publisher Name: Springer, Boston, MA
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