Abstract
Recent studies demonstrated N-(carboxymethyl) lysine (CML) and N-(carboxyethyl) lysine (CEL) in several tissues. To elucidate the mechanism of the formation of advanced glycation end product (AGE) structure during incubation of protein with glucose, we established the quantitative analysis system of CML and CEL by amino acid analyzer with cation exchange and post column ninhydrin detection system and applied for the detection of CML and CEL in AGE structure. We found the formation of CML from Amadori product by the reaction of Fe2+ with H2O2. Further, the formation of CEL in glucose-modified proteins was inhibited by aminoguanidine but enhanced by phosphate.
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