Glycosylated hemoglobins: increased glycosylation of hemoglobin A in diabetic patients

Abstract

The components of the hemoglobin-A1 fraction —hemoglobins A1a-c—arise from nonenzymatic glycosylation of hemoglobin A at the β-chain N-terminal amino groups and can be resolved from hemoglobin A by cation exchange chromatography. Glycosylation can also occur at the α-chain N-terminals as well as the E-amino groups of lysine residues of both α- and β-chains; this results in glycosylated species appearing in the hemoglobin-A fraction. In this study, we determined the extent of hemoglobin-A glycosylation using a colorimetric chemical method specific for the detection of ketoamine-linked hexoses in proteins. We demonstrate increased glycosylation of the main hemoglobin-A fraction in diabetic patients, which correlates significantly (r = 0.72, P < 0.001) with the hemoglobin-A, percentage determined by column chromatography in the corresponding hemolysates. This finding provides the basis for the application of this chemical procedure to the measurement of total glycosylation of hemoglobin.