Identification of Carboxymethyllysine Forming Sites by Nonenzymatic Glycation of Human Serum Albumin in Vitro
松本, 孝 ,
山倉, 文幸 ,
重永, 綾子伊藤, 美香
5 , 2016-12-01 , 昭和女子大学近代文化研究所
Human serum albumin（HSA）is an abundant plasma protein and is modified by glucose in plasma. The incubation of HSA with glucose at 37℃ for four weeks resulted in the formation of carboxymethyllysine in 11 sites of lysine residues of HSA（65, 190 . . .Ⅰ, 199, 233, 313, 378 . . .Ⅱ, 402, 432, 519, 525, 573 . . . Ⅲ）. The same experiments without glucose showed no carboxymethyllysine formation. Although early studies established that four lysine residues（Lys199, Lys281, Lys439 and Lys525）had been modified by nonenzymatic glycosylation, carboxymethylations of Lys281 and Lys439 were not detected in this experiment. Most carboxymethylation of lysine residues in HSA was located in domain Ⅲ in our study.