Glycosylated Hemoglobin and Late Complications of Diabetes Mellitus

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Abstract
To the Editor: Glycosylated hemoglobins are products of a nonenzymatic, irreversible Amadori rearrangement between glucose and the N-terminal valine of the beta chains of adult hemoglobin A.1 They constitute at most 10 per cent of the total hemoglobin in normal human beings,2 and their proportion tends to increase in diabetes mellitus in relation to the extent of hyperglycemia. Glycosylated hemoglobins have a greater affinity for oxygen than does hemoglobin A, and therefore they cause a shift to the left in the oxyhemoglobin dissociation curve, resulting in a decreased availability of oxygen to tissues. This phenomenon may explain the observed hypoxic . . .

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