![]() ‘‘fast’’ is derived from the fact that these components elute faster from a cation-exchange column than the other components.Hemoglobin A1c – comprises 4-6% of the total hemoglobin (the most abundant minor hemoglobin component).Hemoglobin A1b – 0.5% of the total hemoglobin.Hemoglobin A1a – 0.5% of the total hemoglobin.Including negatively charged minor components, collectively designated HbA1:.Other minor hemoglobin components may be formed by posttranslational modification of HbA:.Makes up about 97% of most normal human adult hemoglobin.Consists of two α and two β chains (α2β2).Normal adult hemoglobin molecule (HbA):.5-7% with posttranslational modification.HbA1c is formed by the nonenzymatic condensation of glucose and the N-terminal valine residue of the beta-chain. As with all laboratory tests, HbA1c measurements are associated with variability.HbA1c is a measure of the percentage of hemoglobin molecules attached with glucose.Used in guiding therapy in patients with diabetes and prediabetes.Used in diagnosing patients with diabetes and prediabetes.For decades, HbA1c has remained the standard biomarker for glycemic control, providing a measure of glycemic control over the previous 3 month period (the higher the glucose concentrations over the previous 2-3 months, the higher HbA1c will be).HbA1c is formed at a rate dependent on the glucose concentration to which the red blood cell (RBC) is exposed.This reaction is spontaneous, nonenzymatic, and irreversible. HbA1c is formed from hemoglobin A by the addition of a molecule of glucose to the N-terminal valine of one or both of the beta chains. ![]() HbA1c arises from a posttranslational substrate-concentration-dependent reaction:.Hemoglobin A1c (HbA1c also called glycated hemoglobin) is one of several minor adducts of hemoglobin A. ![]()
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