Co-operative binding of concanavalin A to a glycoprotein in lipid bilayers.
Lectin-binding curves are reported for a concanavalin A receptor glycoprotein in lipid bilayers and intact cells. The results are consistent with previous studies of the structurally dissimilar transmembrane glycoprotein, glycophorin. High-affinity lectin binding to model membranes was influenced by the presence of apparently unrelated macromolecules, which we suggest is an example of receptor modulation by local interactions. Furthermore, high-affinity binding to the model membranes displayed characteristics, including positive cooperativity, similar to those seen with intact cells.
D002784:Cholesterol; D003208:Concanavalin A / Q000378:metabolism*; D004134:Dimyristoylphosphatidylcholine; D004910:Erythrocyte Membrane / Q000276:immunology*; D004912:Erythrocytes / Q000276:immunology*; D006801:Humans; D007700:Kinetics; D008051:Lipid Bilayers; D008954:Models, Biological; D010713:Phosphatidylcholines; D011485:Protein Binding; D011952:Receptors, Concanavalin A / Q000378:metabolism*
D008051:Lipid Bilayers; D010713:Phosphatidylcholines; D011952:Receptors, Concanavalin A; D003208:Concanavalin A; D002784:Cholesterol; D004134:Dimyristoylphosphatidylcholine