Nonenzymic glycation of human immunoglobulins does not impair their immunoreactivity.
Diabetic patients have an increased proportion of their immunoglobulins nonenzymically glycated. To investigate the possibility that this may contribute to increased susceptibility to infection, we compared the immunoreactivity of glycated and nonglycated human immunoglobulins against rubella and hepatitis; streptococcal exoenzyme and infectious mononucleosis; human lymphocytotoxic antigens (HLA); and Varicella zoster in terms of antigen-antibody binding, cell agglutination, cytotoxicity, and complement-fixation properties, respectively. We found no evidence to support the supposition that glycated immunoglobulins are functionally impaired.
Morin
L G
LG
Department of Pathology, Emory University School of Medicine, Decatur, GA.
Austin
G E
GE
Rodey
G E
GE
Johnson
J E
JE
D000914:Antibodies, Viral / Q000276:immunology; D003168:Complement Fixation Tests; D003602:Cytotoxicity, Immunologic; D003920:Diabetes Mellitus / Q000276:immunology / Q000378:metabolism; D006031:Glycosylation; D014645:Herpesvirus 3, Human / Q000276:immunology; D006801:Humans; D007136:Immunoglobulins / Q000378:metabolism*; D012409:Rubella / Q000276:immunology
D000914:Antibodies, Viral; D007136:Immunoglobulins