Post-translational modifications of hemoglobin.
Post-translational modifications of hemoglobin can provide special insights into metabolic disorders. A variety of small molecules in health and disease can form covalent adducts with hemoglobin. The most abundant and best understood of these nonenzymatic modifications is the glycosylation of hemoglobin at the N-terminus of the beta chain (Hb AIc) as well as at the N-terminus of the alpha chain and at certain lysine residues. Glycosylated hemoglobins are elevated in diabetics and offer a useful way of monitoring diabetic control. Moreover, non-enzymatic glycosylation of other tissues may contribute significantly to the long term complications of diabetes. Additional minor hemoglobin components can be formed from other small reactive compounds. For example, cyanate, a breakdown product of urea, reacts with hemoglobin to form distinct minor components in red cells of uremic patients. Acetaldehyde can form hemoglobin adducts in red cells of alcoholics. Thus, hemoglobin can be viewed as a "reporter molecule", revealing metabolic perturbations in a variety of diseases.
D001797:Blood Protein Electrophoresis; D002852:Chromatography, Ion Exchange; D006442:Glycated Hemoglobin / Q000032:analysis / Q000096:biosynthesis / Q000378:metabolism*; D006801:Humans; D007525:Isoelectric Focusing; D011499:Protein Processing, Post-Translational
D006442:Glycated Hemoglobin