UCSF

Univalent antibody fragments prepared from a rabbit antiserum raised against whole human platelets completely inhibited adhesion of platelets to immobilized trimeric collagen in a defined, Mg2+-dependent, adhesion assay. An octylglucoside extract of whole platelets completely neutralized this antibody, and all neutralizing activity bound to immobilized wheat germ agglutinin. Further fractionation on concanavalin A gave rise to subfractions that each neutralized only partially at saturation, when tested against antibody concentrations that inhibit 50% of platelet-collagen adhesion. When tested against higher antibody concentrations that completely inhibited adhesion, each subfraction had no detectable neutralizing effect, although the combined subfractions neutralized completely. This and other evidence suggests that more than one platelet entity participates in platelet-collagen adhesion. Although distinct, they appear to play interdependent roles in a single adhesion process.