Scatchard analysis of the binding of homologous plasma low density lipoproteins (LDL) to human blood platelets shows the existence of a uniform class of saturable specific binding sites. Platelets from healthy donors bound 1470 +/- 640 molecules of LDL per platelet, the constant of association Ka = (6.2 +/- 2.2) X 10-7 l x mol-1. Binding kinetics, temperature dependence, and experiments with formaldehyde-fixed platelets showed that internalization of LDL (at least the labelled apoprotein moiety) did not occur to any considerable degree under the experimental conditions employed. Both very low density lipoproteins (VLDL) and high density lipoproteins 3 (HDL3) markedly inhibited the binding of LDL. In contrast to LDL, HDL3 bound to 3200 +/- 410 binding sites per platelet with a Ka = (9 +/- 1.7) X 10(7) l x mol-1. Additionally, the results of inhibition experiments using both LDL and HDL3 in combination gave evidence, that the sites for HDL3 binding were not identical with those for LDL binding and each inhibited binding of the other noncompetitively with reduction of the binding affinity and the number of available binding sites. VLDL bound to the platelet plasma membrane in a nonspecific-nonsaturable way. Possible significances of the presence of specific LDL receptors on the platelet plasma membrane for recognized functions of these blood elements are discussed.