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In order to explain the precise role of fibrinogen in ADP dependent aggregation of platelets, purification of the presumed platelet fibrinogen receptors is required. We, therefore, compared binding of fibrinogen to the intact platelets and their membranes. Fibrinogen, free of plasminogen and vitamin K-dependent factors, was radiolabelled and used as the probe for a receptor in the platelets membranes. Platelet membranes isolated according to Barber and Jamieson /1970/ were used in the binding assay as a suspension in 0.025 N Tris-HCl buffer, pH 7.4, containing 0.14 M NaCl and 0.66 % polyethylene glycol. The binding specificity was determined by test in which cold fibrinogen completely inhibited binding of the io- dinated fibrinogen, whereas other proteins did not. The pattern of fibrinogen binding was characteristic for a saturable receptor. Scatchard analysis of the binding indicated a single class of receptors, with an estimated association constant of 5 × 108M-1 comparable to that estimated for fibrinogen binding to the intact pig platelets. In contrast to the intact platelets, binding of fibrinogen was not dependent upon the ADP stimulation. We conclude that a specific receptor for fibrinogen is exposed on the surface as a result of cell damage which is the first step of platelet membrane isolation procedure.The isolated membranes retain binding properties of the intact platelets and may serve as a source for the isolation of fibrinogen receptors.

Comparison Op Fibrinogen Binding To Pig Intact Platelets And Their Membranes