Abstract
The Maillard reaction, popularly known as nonenzymatic glycosylation (NEG) or glycation, is a complex chemical reaction and occurs in vivo between reactive aldose or ketose sugars and protein-bound free amino groups (1). NEG has been implicated in diabetic or age-related complications (2), Alzheimer’ disease (3), and also in cataract formation (4). In vivo, any protein with free amino groups can react with reducing sugars via the Maillard reaction. However, the extent of damage caused by NEG is amplified in diabetic tissues (because of the elevated levels of blood sugar levels) and also in proteins with a long half-life like collagen and lens crystallin proteins (1,2). Therefore, determination of early glycation products and protein crosslinks produced because of glycation will be a significant aspect to investigate the extent of damage caused by NEG in vivo.
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Prabhakaram, M., Ortwerth, B.J., Smith, J.B. (2001). Determination of Early Glycation Products by Mass Spectrometry and Quantification of Glycation Mediated Protein Crosslinks by the Incorporation of [14C]lysine into Proteins. In: Cooper, C., Packer, N., Williams, K. (eds) Amino Acid Analysis Protocols. Methods in Molecular Biology™, vol 159. Humana Press. https://doi.org/10.1385/1-59259-047-0:245
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DOI: https://doi.org/10.1385/1-59259-047-0:245
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