FACTORS AFFECTING THE BINDING OF GLYCOPROTEINS TO CONCANAVALIN-A AND RICINUS-COMMUNIS AGGLUTININ AND THE DISSOCIATION OF THEIR COMPLEXES

The association between the glycoproteins, ceruloplasmin (both native and desialylated) and thyroglobulin, and the matrix-bound lectins, concanavalin A and Ricinus communis agglutinin, occurred preferentially at pH 5. All binding was rapid at the temperatures studied, but varied with ionic strength. The capacity of the immobilized lectins varied, on a weight basis, in the fairly narrow range of 0.8 to 3.0 mg glycoprotein per milligram of lectin, although they expressed characteristic and 10-fold different binding capacities on a molar basis. Dissociation of the lectin-glycoprotein complex by simple glycosides was dependent upon time, temperature, and glycoside concentration. © 1979 Academic Press, Inc.