@article{oai:phoenix.repo.nii.ac.jp:00000651,
 author = {高村, 徳人 and Takamura, Norito and 徳永, 仁 and Tokunaga, Jin and 緒方, 賢次 and Ogata, Kenji and 古屋, 弓子 and 本屋, 敏郎 and 松岡, 俊和 and 平井, 正巳 and 西尾, 豊隆 and 川井, 恵一 and 有森, 和彦 and タカムラ, ノリト and トクナガ, ジン and オガタ, ケンジ and フルヤ, ユミコ and モトヤ, トシロウ and マツオカ, トシカズ and ヒライ, マサミ and ニシオ, トヨタカ and カワイ, ケイイチ and アリモリ, カズヒコ and TAKAMURA, Norito and TOKUNAGA, Jin and OGATA, Kenji and FURUYA, Yumiko and MOTOYA, Toshiro and MATSUOKA, Toshikazu and HIRAI, Masami and NISHIO, Toyotaka and KAWAI, Keiichi and ARIMORI, Kazuhiko},
 journal = {九州保健福祉大学研究紀要, Journal of Kyushu University of Health and Welfare},
 month = {Mar},
 note = {P(論文), The interaction of uremic toxins, indoxyl sulfate (IS), indoleacetic acid (IA) 3-carboxy-4-methyl-5-propyl-2-furanpropanoic acid (CMPF), with human serum albumin (HSA) was investigated by ultrafiltration and spectroscopic methods including ultra violet and fluorescence probe method. The primary binding site of IA and IS was designated site II, and the CMPF binding site was site I on the HSA molecule, as indicated by displacement experiments using different site-selective probes. Tyrosine (Tyr) and lysine (Lys) amino acid residues were probably involved in the binding sites of uremic toxins (IS, IA, CMPF) to HSA. Both hydrophobic and electrostatic interactions were found to play a role in the binding of uremic toxins to HSA. Binding of CMPF was sensitive to the N-B transition of HSA. It is suggested that the binding sites consist of a cationic site on the surface of the HSA molecule with a hydrophobic crevice to accommodate the aromatic ring of the uremic toxins. The results obtained in this study will be useful for the exact understanding of the characteristics of protein binding sites of uremic toxins.},
 pages = {211--215},
 title = {尿毒症物質の血清蛋白結合の特性に関する研究},
 volume = {7},
 year = {2006},
 yomi = {タカムラ, ノリト and トクナガ, ジン and オガタ, ケンジ and フルヤ, ユミコ and モトヤ, トシロウ and マツオカ, トシカズ and ヒライ, マサミ and ニシオ, トヨタカ and カワイ, ケイイチ and アリモリ, カズヒコ}
}