Determination of the non-enzymatic glycation of hemoglobin by isoelectrofocusing of its globin chains.
Micro cation exchange chromatography determination of HbA1c does not provide a complete picture of Hb glycation, for it does not determine all the glycated forms of hemoglobin. For the determination of total glycation, we describe here a rod IEF method, which allows the simultaneous quantitation of glycation on alpha and beta globin chains. The method exhibits good sensitivity; it is not affected by artifacts deriving from temperature, hypertriglyceridemia, Hb variants or labile HbA1 (aldiminic Hb). The results obtained indicate that in a normal population approximately 18% of the beta chain and 8% of the alpha chain are glycated. These mean percentages increase in the diabetic to 28% and 12%, respectively. The beta chain is glycated on both valine and lysine residues, while the alpha chain is glycated only on the latter. HbA1 values from micro cation exchange chromatography are significantly related to both alpha and beta glycation. Thus, valinic or lysinic glycation have roughly the same clinical significance.
D003920:Diabetes Mellitus / Q000175:diagnosis / Q000378:metabolism; D005947:Glucose / Q000378:metabolism; D006442:Glycated Hemoglobin / Q000032:analysis*; D006441:Hemoglobin A / Q000032:analysis; D006801:Humans; D007475:Ion Exchange Resins; D007525:Isoelectric Focusing / Q000379:methods*
D005947:Glucose; D006442:Glycated Hemoglobin; D006441:Hemoglobin A; D007475:Ion Exchange Resins