Distribution of receptor sites on large glycoprotein molecules by electron microscopy. Application to epiglycanin.
Electron microscopy was used to map the loci of immunochemically active sites on individual glycoprotein molecules. The positions of specific galactose residues and asparagine-linked carbohydrate chains containing specific mannose residues in epiglycanin, a glycoprotein of extended conformation from the surface of TA3 mouse mammary tumour cells, were observed in complexes with Ricinus communis toxin and concanavalin A respectively. The maximum number of Ricinus communis toxin molecules attached to a single epiglycanin molecule was 23, and the average number was 16. Only one concanavalin A molecule was observed attached to any epiglycanin molecule, and this at one end of the molecule, suggesting the presence of only one receptor for this lectin. By means of this new approach for mapping specific residues, evidence has been obtained that suggests microheterogeneity in epiglycanin with respect to the locations of carbohydrate chains containing receptors for Ricinus communis toxin.
D000818:Animals; D001665:Binding Sites; D055598:Chemical Phenomena; D002621:Chemistry; D006023:Glycoproteins / Q000378:metabolism*; D046911:Macromolecular Substances; D008562:Membrane Glycoproteins; D051379:Mice; D008854:Microscopy, Electron; D011485:Protein Binding; D011952:Receptors, Concanavalin A / Q000032:analysis; D011975:Receptors, Mitogen / Q000378:metabolism
D006023:Glycoproteins; D046911:Macromolecular Substances; D008562:Membrane Glycoproteins; D011952:Receptors, Concanavalin A; D011975:Receptors, Mitogen; C032650:Ricinus communis lectin receptor; C016424:epiglycanin protein, mouse