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- W1199540836 abstract "This chapter summarizes the glycosylation of proteins by nonenzymatic processes in humans and related species. The prototype molecule for this process must be considered to be hemoglobin AIc (Hb AIc), as this was the first protein recognized to be nonenzymatically glycosylated. Glucose reacts to form a schiff base with NH2-terminus of the β chain of Hb A, and subsequently undergoes an amadori rearrangement to yield 1-amino- 1-deoxyfructose. This modified hemoglobin, named Hb AIc, is a normal red cell constituant present in increased concentration in patients with diabetes mellitus. Hb AIc is synthesized throughout the life of the erythrocyte in a slow, nearly irreversible raction. The rate of synthesis is a function of blood glucose concentration. These properties of Hb AIc combine to make it an indicator molecule whose concentration at one point in time reflects the patient's mean blood glucose level for the preceding month. This gives Hb AIc a unique and invaluable role in clinical medicine, for it is the only known parameter that accurately assesses long term carbohydrate control. While Hb AIc itself is not likely to have deleterious effects, the nonenzymatic glycosylation of other proteins may result in altered enzymatic activity, solubility, antigenicity etc., and thereby result in many of the clinical sequelae of long-standing diabetes. In this regard, lens proteins undergo increased glycosylation in high carbohydrate environments, and such glycosylation increases the ease with which the proteins oxidize to form high molecular weight aggregates and opacities. In fact, nonenzymatic glycosylation may play a major role in the normal aging process as the complications of diabetes are frequently considered to resemble accelerated aging." @default.
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- W1199540836 date "1979-01-01" @default.
- W1199540836 modified "2023-09-23" @default.
- W1199540836 title "Chapter 25 Non-enzymatic Glycosylation" @default.
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- W1199540836 doi "https://doi.org/10.1016/s0065-7743(08)61370-6" @default.
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