A characterization of the BALB/c lambda and kappa class antibodies to alpha (1,3) glycosidic linkages.
The avidity relationships of kappa and lambda antibodies with specificity for the glucosyl-alpha (1,3)-glucose disaccharide epitope were compared using a solid-phase hapten inhibition assay. The kappa class antibodies, induced by the T-cell-dependent antigen, nigerosyl-keyhole limpet hemocyanin (N-KLH), and the lambda class antibodies, induced by the T-cell-independent antigen, Dextran B1355, were only marginally distinguishable (approximately equal to 10-fold) on the basis of hapten inhibition using the free disaccharide, nigerose, as inhibitor. Analysis of the binding site sizes of antibodies induced by N-KLH through inhibition with oligosaccharides of different sizes showed that the disaccharide protein antigen did not select for antibodies with smaller binding site sizes. The cellular basis for these findings is discussed.
D000818:Animals; D000906:Antibodies / Q000276:immunology*; D001665:Binding Sites; D003911:Dextrans / Q000276:immunology; D004187:Disaccharides / Q000276:immunology*; D000939:Epitopes / Q000032:analysis; D006433:Hemocyanins / Q000276:immunology; D007075:Immunoglobulin M / Q000276:immunology; D007145:Immunoglobulin kappa-Chains / Q000276:immunology*; D007146:Immunoglobulin lambda-Chains / Q000276:immunology*; D051379:Mice; D008807:Mice, Inbred BALB C; D009844:Oligosaccharides / Q000494:pharmacology; D013601:T-Lymphocytes / Q000276:immunology
D000906:Antibodies; D003911:Dextrans; D004187:Disaccharides; D000939:Epitopes; D007075:Immunoglobulin M; D007145:Immunoglobulin kappa-Chains; D007146:Immunoglobulin lambda-Chains; D009844:Oligosaccharides; D006433:Hemocyanins; C032808:keyhole-limpet hemocyanin