title: Nonenzymatic glycation of immunoglobulins does not impair antigen-antibody binding.
abstract: 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.
mesh_terms: 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
chemical_list: D000906:Antibodies; D000941:Antigens; D007136:Immunoglobulins; D011933:Reagent Kits, Diagnostic; D013858:Thiobarbiturates; D014168:Transferrin; D013972:Thyrotropin; D005293:Ferritins; D005947:Glucose; C029684:thiobarbituric acid