The asymmetric IgG non-precipitating antibody. Localization of the oligosaccharide involved, by concanavalin A interaction.
Binding to Con A-Sepharose 4B of the low-affinity Fab fragment from sheep IgG1 anti-Dnp non-precipitating antibody was previously determined. This communication reports the results obtained when the concanavalin A interaction with Fd' fragments and L chains from non-precipitating and precipitating antibodies was examined. When Fd' fragments and L chains from non-precipitating and precipitating antibodies were tested as inhibitors of the binding of 125I-labelled concanavalin A to guinea pig erythrocytes, inhibition of such binding was only achieved by Fd' fragments from non-precipitating antibodies. Forty eight per cent of this Fd' fragment was bound by Con A-Sepharose 4B. From these results and our previous studies we conclude that mannose and/or glucose residues must be present and exposed at the Fd' fragment from the low-affinity Fab arm of sheep IgG1 anti-Dnp non-precipitating antibody. Glycosylation differences may explain the difference in precipitation behaviour of the 2 types of antibody.
D000818:Animals; D001667:Binding, Competitive; D055598:Chemical Phenomena; D011232:Chemical Precipitation; D002621:Chemistry; D002846:Chromatography, Affinity; D003208:Concanavalin A / Q000276:immunology*; D006168:Guinea Pigs; D007128:Immunoglobulin Fragments / Q000276:immunology; D007074:Immunoglobulin G / Q000276:immunology*; D009844:Oligosaccharides / Q000032:analysis*; D012756:Sheep
D007128:Immunoglobulin Fragments; D007074:Immunoglobulin G; D009844:Oligosaccharides; D003208:Concanavalin A