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- W2889486407 abstract "Binding of fibrinogen by thrombin was measured by inhibition of amidolysis of S2238 and found to be 12 μM. Upon digestion of fibrinogen with plasmin (0.16ugs/mg fibrinogen) for 4 hours at 37°C, thrombin binding activity remained in the supernatants upon heat treatment. The thrombin binding activity in the dialyzed supernatant reached a maximum after two hours coinciding with maximal release of B 1-42 and 45-39 KDa chain fragments. Measured immunologically, levels of fragment E at this time were 45% of the maximum generated after 4 hours digestion. FPA levels in the dialyzed supernatant (measured by RIA and HPLC) after thrombin treatment, were zero and did not increase until 1½ hours after the beginning of digestion, reaching a maximum at 4 hours. The thrombin binding activity generated was stable to further plasmin action. Upon gel chromatography of 2 and 4 hour supernatants, thrombin binding activity coincided closely with fragment E, measured immunologically. Further purification showed the fragment to have Ki for thrombin amidolytic activity of 0.5μM. The fragment also inhibited the thrombin clotting time of plasma but did not affect fibrin monomer polymerization.The fragment was susceptible to very slow inactivation by thrombin but not arvin (though it did inhibit arvin amidolytic activity). A thrombin binding (thrombin inhibitory) fragment is therefore generated during the early stages of f ibrinogenolysis and may be the result of protection by 45 and 39 KDa A α carboxy terminus fragments since E fragments generated in later stages (in the presence of 29 and 25 KDa fragments) do not have this property. These findings may give interesting new insight into thrombin/fibrinogen interaction." @default.
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- W2889486407 date "1987-01-01" @default.
- W2889486407 modified "2023-09-23" @default.
- W2889486407 title "THROMBIN BINDING FRAGMENT E GENERATED DURING FIBRINOGENOLYSIS" @default.
- W2889486407 doi "https://doi.org/10.1055/s-0038-1642937" @default.
- W2889486407 hasPublicationYear "1987" @default.
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