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Incubation of fibrinogen Seattle II with thrombin (17 mu/ml) resulted in the release of two forms of fibrinopeptide A (FpA) which were resolved by high-performance liquid chromatography. Amino acid analysis disclosed that the abnormal FpA contained histidine in place of arginine. At lower, approximately physiologic thrombin concentrations only half the normal amount of FpA was released, and fibrinopeptide B (FpB) release was delayed. The effect of this substitution on the time course of fibrinopeptide release is consistent with conclusions drawn from other studies on the kinetics of fibrinopeptide release, viz., that prior removal of FpA is not required before FpB hydrolysis by thrombin, and that optimal rates of FpB release occur after formation of fibrin I polymer.
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W E Schreiler, and
W R Bell
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R F Ebert, and
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