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ID 114775
著者
Mine, Masanori Tokushima University
キーワード
Capillary electrophoresis
Dynamic frontal analysis
β-D-galactosidase
Substrate competition
Michaelis-Menten constant
Inhibition constant
資料タイプ
学術雑誌論文
抄録
Competitive inhibition between two substrates with an enzyme is investigated by capillary electrophoresis/dynamic frontal analysis (CE/DFA). Enzymatic hydrolyses of o-nitrophenyl β-D-galactopyranoside and p-nitrophenyl β-D-galactopyranoside with β-D-galactosidase were examined as a model competitive reaction. A sample solution containing the two substrates was injected into a capillary filled with a separation buffer containing an enzyme. Enzymatic hydrolysis occurred during the electrophoresis, and the products of o-nitrophenol and p-nitrophenol were continuously formed and resolved from the sample zone. Two-steps plateau signal was detected with the two-substrate solutions based on the difference in the effective electrophoretic mobility of o-nitrophenol and p-nitrophenol. Michaelis-Menten constants and inhibition constants were determined with the plateau heights. Usefulness of CE/DFA on competitive inhibition analysis is demonstrated in this study.
掲載誌名
Journal of Pharmaceutical and Biomedical Analysis
ISSN
07317085
cat書誌ID
AA10644220
AA11533870
出版者
Elsevier
188
開始ページ
113390
発行日
2020-05-29
備考
論文本文は2022-05-29以降公開予定
権利情報
© 2020. This manuscript version is made available under the CC-BY-NC-ND 4.0 license http://creativecommons.org/licenses/by-nc-nd/4.0/
EDB ID
出版社版DOI
出版社版URL
言語
eng
著者版フラグ
その他
部局
理工学系