Comparison of the Cross-Linking Patterns of Lamprey Fibrinogen and Fibrin by the Action of the Intrinsic Lamprey Factor XIII and Human Factor XIII during the Process of Blood Coagulation

Summary

Intrinsic lamprey factor XIII cross-links the γ-chain of lamprey fibrin (50,000 daltons) to the γ-dimer (100,000 daltons). The a-chain (110,000 daltons) is cross-linked very slowly to a-dimer (210,000 daltons) and a-trimer (330,000 daltons). In contrast, human factor XIII, when added in combination with intrinsic lamprey factor XIII, cross-finks the a-chain of lamprey fibrin to a high molecular weight polymer, and any remaining γ-chain is also cross-linked to a polymer. However, the γ-chain that has previously cross-linked to the γ-dimer by the intrinsic lamprey factor XIII remains as a γ-dimer. Factor XIII-free lamprey fibrin cross-links all its subunits (α, β, γ) to high molecular weight polymers when human factor XIII is added. In contrast to human and bovine fibrin where α-chain cross-linking in the process of blood coagulation commences when all of the γ-chain has cross-linked, the lamprey α-chain will begin to cross-link when approximately half of the γ-chain has cross-linked to the γ-dimer.

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