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Interactions of lectins with membrane glycoproteins effects of concanavalin A on 5′-nucleotidase
Authors:JR Riordan  M Slavik
Institution:Department of Biochemistry Research, Research Institute, The Hospital for Sick Children, Toronto, Ontario Canada
Abstract:Concanavalin A causes a biphasic modification of the activity of the plasma membrane enzyme 5′-nucleotidase. The first stimulatory phase occurs from 0 to 0.05 μM concanavalin A, the second inhibitory phase at higher concentrations. The curve relating binding of 125I-labelled concanavalin A and concentration of native lectin is similarly biphasie. The two phases likely result from occupation of distinct families of binding sites. When the enzyme is extracted from the membrane, the stimulatory phase disappears. Thus, the high affinity binding sites responsible for this phase depend upon the intact membrane structure while the others do not.
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