Glycation Lab Report

ADVANCED GLYCATION END PRODUCTS

Advanced glycation end product as an oxidative process that occurred in food perserved or heated the presence of reducing sugars were first observed in early 1900s which non-enzymatically make the food proteins insoluble with yellowish fluorescent products attached to them. This process is known as Maillard reaction named on its discoverer the Louis C. Maillard in 1912 (Finot ., 2005). The Maillard reaction is the one of physiological significance. In vivo, it is also observed that human protein non-enzymatically glycated in the presence of physiologic sugars. One of the best characterized glycation product known to occur in the body is glysocylated hemoglobin. Raised AGE accumulation is not only confined to

The amino side chain most encountered to this reaction are valine,lysine and arginine which lead to the formation of Schiff bases at the rate proportional to concerntration to sugars which undergoes amadori rearrangement to form a stable glycation end-product (brownlee et al., 1988) which accumulates in long lived tissue proteins causing cross linking and develop inflammation and thickening of basement membrane leading to complication like retinopathy, neuropathy, nephropathy and atherosclerosis

Upon its discovery, HbA1c was proposed as a useful biomarker for diabetes monitoring (Koenig et al., 1976a, Koenig et al., 1976b), and endogenously produced AGEs attracted further scientific attention, beyond food chemistry, from fields including medical biochemistry and pathology. At this point it is important to highlight that there are two sources of AGEs: the endogenously produced AGEs, a product of the reaction between proteins and sugars in the circulation, and exogenous AGEs, produced during cooking and absorbed in the small intestine (~10%