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- W2024142077 abstract "The binding of human factor Xa to fibrinogen and its derivatives was characterized. Factor Xa bound to immobilized fibrin with a concentration at half‐maximal binding (C 50 ) of 100nM. The 4‐carboxyglutamic acid (Gla) domain of factor Xa is important in factor Xa binding to fibrin monomer, based on the following observations; the binding requires Ca 2+ ; Gla‐domain‐lacking factor Xa could not bind to fibrin; factor Xa binding was significantly reduced by prior treatment of factor Xa with factor IX/factor‐X‐binding protein from the venom of Trimeresurus flavoviridis which specifically binds to the Gla domain of human factors IX and X. Factor Xa also bound to fibrinogen, fibrinogen degradation products (FDP)‐D and FDP‐E, with a similar affinity (C 50 = 75–131 nM). In a solution‐phase equilibrated binding assay, approximately 0.76 mol factor Xa bound to 1 mol fibrinogen with a dissociation constant of 180 nM. The binding of 125 I‐labeled factor Xa to the fibrin monomer was inhibited markedly by unlabeled factor Xa, but only slightly by thrombin, suggesting that the binding site of factor Xa on fibrin monomer differs from that of thrombin. We localized the binding site of factor Xa on fibrinogen: factor Xa bound strongly to the Aα chain, but weakly to the Bβ and γ chains of fibrinogen. The Aα chain was then digested with lysyl endopeptidase and separated by reverse‐phase HPLC. Among resulting peptides, factor Xa bound specifically to a peptide corresponding to residues Asp82–Lys123 of the Aα chain. This factor‐Xa‐binding site is located in the boundary between the central E domain and the terminal D domain of fibrinogen and is apparently distinct from the reported thrombin‐binding site." @default.
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- W2024142077 date "1995-08-01" @default.
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- W2024142077 title "Characterization of the Binding of Factor Xa to Fibrinogen/Fibrin Derivatives and Localization of the Factor Xa Binding Site on Fibrinogen" @default.
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- W2024142077 doi "https://doi.org/10.1111/j.1432-1033.1995.tb20785.x" @default.
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