The effect of a collagen-derived octapeptide on some properties of thrombin is presented. This peptide provoked a dose- and time-dependent prolongation of the thrombin-induced plasma and fibrinogen clotting time and inhibited the polymerization of fibrin generated from fibrinogen by thrombin. It did not affect the polymerization of fibrin monomers; it was also without effect on the coagulation of plasma or fibrinogen by reptilase. The prolongation of the fibrinogen clotting time depended on the duration of the incubation of thrombin and the octapeptide and not on the duration of the incubation of fibrinogen and the octapeptide. The inhibition was therefore ascribed to an interference with thrombin, rather than with fibrinogen. A preincubation of the octapeptide with thrombin resulted in an inhibition of the thrombin-induced platelet aggregation. The effect of the octapeptide on thrombin has been related to the presence of positively and negatively charged groups, because uncharged analogue sequences were without effect on these activities of thrombin.

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