Abstract
The nonenzymatic interaction of glucose with amino groups of proteins and amino acids results in generation of stable products. This post-translational nonenzymatic modification of proteins and amino acids is called glycosylation [1]. The glycosylation occurs due to a small fraction of glucose (about 0.002% of the total amount) which is in the opened (aldehyde) form and produces the reversible Schiff bases with amino groups of proteins or amino acids. This base changes to the stable adduct, ketoamine, due to the intramolecular Amadori rearrangement [2]. Further incubation results in the generation of a number of cyclic compounds with absorption in the near UV and visible regions of the spectrum and a rather intense fluorescence [2, 3]. Among the colored cyclic products, derivatives of furanyl imidazole have been identified [4, 5].
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© 1999 Springer Science+Business Media Dordrecht
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Stepuro, I.I., Chaikovskaya, N.A. (1999). Interaction of glycosylated amino acids with human serum albumin. In: Greve, J., Puppels, G.J., Otto, C. (eds) Spectroscopy of Biological Molecules: New Directions. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-4479-7_17
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DOI: https://doi.org/10.1007/978-94-011-4479-7_17
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