The Affinity of Concanavalin A and 'Lens culinaris' Hemagglutinin for Glycopeptides,
NATIONAL RESEARCH COUNCIL OF CANADA OTTAWA (ONTARIO) DIV OF BIOLOGICAL SCIENCES
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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 1,000,000. 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 constrast, in another precipitation system, Lens culinaris hemagglutinin was inhibited by glycopeptides from transferrin and IgM but not by the ovalbumin glycopeptides.