The affinity of concanavalin A and Lens culinaris hemagglutinin for glycopeptides

Abstract The affinity of concanavalin A for ovalbumin, transferrin and glycopeptides from these proteins and from IgM has been investigated by studying inhibition of a concanavalin A-dextran precipitation system. The mixture of glycopeptides from ovalbumin was a powerful inhibitor with an apparent association constant above 10 6 . The parent glycoprotein was a poorer inhibitor, but capable of forming soluble complexes of sufficient stability for isolation by gel filtration. The other inhibitors were also of high avidity. In contrast, in another precipitation system, Lens culinaris hemagglutinin was inhibited by glycopeptides from transferrin and IgM (apparent association constant close to 10 5 ) but not by the ovalbumin glycopeptides.