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- W2034622062 abstract "The binding of thrombin activated 125I labeled N-DSK (N-DSKXa) to thrombin activated fibrinogen-Sepharose (Fbm-Sepharose) wasa studied. The competition with N-DSKXa of N-DSK, N-DSKa, fibrinogen, plasmin fragments Ds and E, fibrinopeptides A and B and the tryptic core fragment of N-DSK (DS-4) is reported. A minimum of one non-interacting site was observed for the binding of N-DSKa to FbmSepharose. The binding constant was 2.2 × 105M−1 and the Hill coefficient, 0.87. N-DSK activated with Reptilase (R/N-DSK) had only half the affinity of N-DSK. Fragment E, after thrombin activation, had an affinity comparable to R/N-DSK. Fibrinogen and fragment Ds were also strong inhibitors of N-DSKxa binding, most probably by interaction with N-DSKxa in solution. The fibrinopeptides, N-DSK before thrombin activation, and DS-4 were poor antagonists of N-DSKa binding to Fbm-Sepharose." @default.
- W2034622062 created "2016-06-24" @default.
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- W2034622062 date "1976-05-01" @default.
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- W2034622062 title "Interaction of fragments of fibrinogen with insolubilized fibrin monomers (activated fibrinogen)" @default.
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- W2034622062 doi "https://doi.org/10.1016/0049-3848(76)90242-5" @default.
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