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Updated: Aug 8, 2026

Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases
Published on: December 26, 2011
Abstract:
Nonenzymatic glycosylation takes place in all proteins with a free-reacting lysine or valine in the presence of glucose. The formation of glycosylated plasma albumin, hemoglobin (Hb A1c), and skin collagen provides a diagnostic index of short- to long-term time-concentration of glucose in vivo. A wide range of assay methods are available, with affinity chromatographic, isoelectric focusing, and spectrophotometric methods providing the best accuracy and versatility. Glycosylated hemoglobin assays indicate glucose pressure over the previous 2 to 3 months and are of diagnostic value in general diabetic control, while glycosylated plasma albumin determinations are preferable in acute episodes in the life of a diabetic (e.g., pregnancy, infection, stress, trauma, surgery), since they provide an overview of changing blood glucose values of the previous 2 to 4 weeks. Glycosylated collagen estimations reflect tissue aging and are relevant in healing processes. Glycosylation alters the biologic activity of proteins, and these may relate to the manifold complications concomitant on the lifelong elevation of blood and tissue glucose in the diabetic (C6a). Assays for glycosylated hemoglobin have been routinely performed in clinical chemistry laboratories for a decade, and convenient determination for other nonenzymatically glycosylated proteins is proceeding apace.
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