α-Glucosidase inhibition assay in an enzyme-immobilized amino-microplate

Toshiro Matsui, Mayu Shimada, Nozomi Saito, Kiyoshi Matsumoto

研究成果: Contribution to journalArticle査読

12 被引用数 (Scopus)

抄録

α-Glucosidase (AGH) from the small intestine of rat was immobilized onto a glutaradehyde (GA) activated NH2-96 well microplate to establish a convenient and rapid AGH inhibition assay system. After AGH immobilization, remaining GA groups were blocked by β-alanine to induce a negative charge on the surface of the well. The AGH-plate showed an enzyme activity of 444 nU/well under an assayed condition at 37°C for 2 h using 0.3 mM 4-methylumbelliferyl-α-D- glucopyranoside as a fluorogenic substrate. Inhibitory powers of voglibose and acarbose as therapeutic AGH inhibitors were successfully evaluated to have IC50 values of 13 and 114 nM, respectively. 2009

本文言語英語
ページ(範囲)559-562
ページ数4
ジャーナルanalytical sciences
25
4
DOI
出版ステータス出版済み - 4 2009

All Science Journal Classification (ASJC) codes

  • 分析化学

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