Nonenzymatic glycation of immunoglobulins does not impair antigen-antibody binding.
We glycated immunoglobulins from commercial kits designed to measure human ferritin, thyrotropin, and transferrin, and compared the calibration curves for assays utilizing glycated antibodies with those of assays utilizing non-glycated antibodies. Glycation was verified by borate affinity chromatography and assay with thiobarbituric acid reagent. We found no evidence that antigen-antibody binding is impaired by nonenzymatic glycation of antibodies. Our results provide no evidence in support of the supposition that glycation may be a contributory factor in the decreased resistance of diabetics to infection.
D000906:Antibodies / Q000276:immunology; D000937:Antigen-Antibody Reactions; D000941:Antigens / Q000276:immunology; D002846:Chromatography, Affinity; D003920:Diabetes Mellitus / Q000276:immunology; D005293:Ferritins / Q000032:analysis; D005947:Glucose / Q000378:metabolism*; D006031:Glycosylation; D006801:Humans; D007136:Immunoglobulins / Q000276:immunology / Q000378:metabolism*; D011933:Reagent Kits, Diagnostic; D013858:Thiobarbiturates; D013972:Thyrotropin / Q000032:analysis; D014168:Transferrin / Q000032:analysis
D000906:Antibodies; D000941:Antigens; D007136:Immunoglobulins; D011933:Reagent Kits, Diagnostic; D013858:Thiobarbiturates; D014168:Transferrin; D013972:Thyrotropin; D005293:Ferritins; D005947:Glucose; C029684:thiobarbituric acid