@article{oai:swu.repo.nii.ac.jp:00000385,
 author = {松本, 孝 and 山倉, 文幸 and 重永, 綾子 and 伊藤, 美香 and MATSUMOTO, Takashi and YAMAKURA, Fumiyuki and SHIGENAGA, Ayako and ITOH, Mika},
 issue = {914},
 journal = {学苑, Gakuen},
 month = {Dec},
 note = {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.},
 pages = {1--5},
 title = {〔研究ノート〕ヒト血清アルブミンの糖化反応による カルボキシメチルリジンの生成箇所の同定},
 year = {2016},
 yomi = {マツモト, タカシ and ヤマクラ, フミユキ and シゲナガ, アヤコ and イトウ, ミカ}
}