The binding of highly purified bovine coagulation factor Xa to washed bovine platelets was studied. 125I-labeled factor Xa underwent binding to a platelet receptor that became accessible only after induction of the platelet release reaction by thrombin or by the calcium ionophore A 23187. The zymogen factor X did not bind to platelets. The factor Xa binding was saturable, reversible, and correlated with the rate of thrombin formation. The number of factor Xa binding sites per platelet was 290--420 and the apparent association constant was estimated to be 2.8 x 109 to 1.0 x 1010 M-1. Diisoprophyl fluorophosphate-factor Xa bound to the same platelet receptor as factor Xa indicating that limited proteolysis of a receptor protein was not required for binding. The rate of factor Xa binding was rapid (2.1 x 10(6) to 2.9 x 10(6) M-1 s-1) and similar to that preveiously found for the rate of binding of polypeptide hormones to their receptors. Displacement of factor Xa from the platelet receptor by diisopropyl fluorophosphate-factor Xa effectively blocked thrombin formation. Low concentrations of factor Xa catalyze prothrombin activation more effectively in the presence of platelets than in the presence of phospholipid and factor V.