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ID 114775
Author
Mine, Masanori Tokushima University
Keywords
Capillary electrophoresis
Dynamic frontal analysis
β-D-galactosidase
Substrate competition
Michaelis-Menten constant
Inhibition constant
Content Type
Journal Article
Description
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.
Journal Title
Journal of Pharmaceutical and Biomedical Analysis
ISSN
07317085
NCID
AA10644220
AA11533870
Publisher
Elsevier
Volume
188
Start Page
113390
Published Date
2020-05-29
Remark
論文本文は2022-05-29以降公開予定
Rights
© 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
DOI (Published Version)
URL ( Publisher's Version )
language
eng
TextVersion
その他
departments
Science and Technology