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• W2888877760 abstract "The fibrinopeptides A and B (FPA and FPB) are cleaved from the fibrinogen molecule with different rates. In the initial phase of the thrombin-fibrinogen reaction, FPB is released with a slow rate, which is enhanced upon polymerization of desA-fi-brin monomers. The aim of the present study was to further characterize the mechanism leading to the enhanced rate of FPB release during polymerization. For this purpose, the release of FPB from normal fibrinogen and from fibrinogen London I, which exhibits a polymerization defect located in the D-domain, was studied in the presence and absence of the fibrinolytic fragment D1 (D1) and of the synthetic tetrapeptide Gly-Pro-Arg-Pro (GPRP). Steady state parameters for fibrinopeptide release were determined under pseudo-first order reaction conditions. In the initial phase of the thrombin-fibrinogen reaction, the release of FPA was unchanged in the presence of D1. Furthermore, the release of FPA from fibrinogen London I did not reveal any difference in comparison to normal fibrinogen. GPRP prevented not only fibrin polymerization, but also the enhanced rate of FPB release. On the contrary, the rate of FPB release in the presence of a 16- and 32-fold molar excess of over fibrinogen did not differ from a reaction mixture with no added D1. Si-miliar to the inhibited rate of FPB release in the presence of GPRP, the release of FPB from fibrinogen London I occurred with a slow rate, which was not enhanced by the addition of a 16-fold molar excess of D1. Since the release neither from normal fibrinogen nor from ribrinogen London I was affected by D1, it was concluded that the D-E contact formed by D1 with an E-domain of a desA-fibrin molecule does not enhance the release of FPB. While GPRP keeps fibrin in monomeric form by inhibiting the polymerization sites in the D-domains, D1 does not prevent the formation of fibrin oligomers. Therefore, acceleration of FPB release is caused by a conformational change, which is induced by binding of reciprocal polymerization sites to an E-as well as a D-domain of the same desA-fibrin molecule." @default.
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• W2888877760 date "1987-01-01" @default.
• W2888877760 modified "2023-09-27" @default.
• W2888877760 title "FIBRINOPEPTIDE B RELEASE FROM NORMAL FIBRINOGEN AND FIBRINOGEN LONDON I IN THE PRESENCE OF INHIBITORS OF FIBRIN POLYMERIZATION" @default.
• W2888877760 doi "https://doi.org/10.1055/s-0038-1643341" @default.
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