@article{oai:tohoku-mpu.repo.nii.ac.jp:00000565,
 author = {色川, 隼人 and Irokawa, Hayato and 三好, 道世 and Miyoshi, Michiyo and 菅原, 大輔 and Sugawara, Daisuke and 岩井, 健太 and Iwai, Kenta and 久下, 周佐 and Kuge, Shusuke},
 issue = {60},
 journal = {東北薬科大学研究誌, Journal of Tohoku Pharmaceutical University},
 month = {Dec},
 note = {Recent studies shed light on a crucial function of M2 isoform of mammalian pyruvate kinase（PkM2）on tumor cell growth. Pyruvate kinase activity of PkM2 was shown to be negatively regulated by growth factors or reactive oxygen species（ros）. The negative regulation of PkM2 enhances tumor cell growth. Despite biochemical and genetic evidences to indicate mechanism for the ros-induced negative regulation of PkM2, an apparent oxidized form of PkM2, which is induced by cellular ros such as H2o2, has not been identified so far. Thus, we aimed to identify oxidized PkM2 in cells in response to H2o2. To identify number of free cysteine thiols, we examined changes of molecular weight shift of PkM2, which is determined by the number of pegylated-maleimide molecule（Mw 2,000）bound to PkM2 thiols. our results suggested that one or two out of nine cysteine residues in PkM2 were oxidized in response to H2o2. our system may be useful to determine changes in PkM2 redox status in cells in response to ros-inducible environmental changes such as oxygen and nutrient availability.},
 pages = {49--54},
 title = {ヒト癌細胞型ピルビン酸キナーゼ（PKM2）の過酸化水素に応答したレドックス状態変化の検出},
 year = {2013},
 yomi = {イロカワ, ハヤト and ミヨシ, ミチヨ and スガワラ, ダイスケ and イワイ, ケンタ and クゲ, シュウスケ}
}