title: 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.
abstract: Intrinsic lamprey factor XIII cross-links the gamma chain of lamprey fibrin (50,000 daltons) to the gamma-dimer (100,000 daltons). The alpha-chain (110,000 daltons) is cross-linked very slowly to alpha-dimer (210,000 daltons) and alpha-trimer (330,000 daltons). In contrast, human factor XIII, when added in combination with intrinsic lamprey factor XIII, cross-links the alpha-chain of lamprey fibrin to a high molecular weight polymer, and any remaining gamma-chain is also cross-linked to a polymer. However, the gamma-chain that has previously cross-linked to the gamma-dimer by the intrinsic lamprey factor XIII remains as a gamma-dimer. Factor XIII-free lamprey fibrin cross-links all its subunits (alpha, beta, gamma) to high molecular weight polymers when human factor XIII is added. In contrast to human and bovine fibrin where alpha-chain cross-linking in the process of blood coagulation commences when all of the gamma-chain has cross-linked, the lamprey alpha-chain will begin to cross-link when approximately half of the gamma-chain has cross-linked to the gamma-dimer.
mesh_terms: D000818:Animals; D001777:Blood Coagulation; D005176:Factor XIII / Q000494:pharmacology*; D005337:Fibrin / Q000378:metabolism*; D005340:Fibrinogen / Q000378:metabolism*; D005399:Fishes / Q000097:blood*; D006801:Humans; D007798:Lampreys / Q000097:blood*; D008970:Molecular Weight
chemical_list: D005337:Fibrin; D005340:Fibrinogen; D005176:Factor XIII