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

Toshiro Matsui, Mayu Shimada, Nozomi Saito, Kiyoshi Matsumoto

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

α-Glucosidase (AGH) from the small intestine of rat was immobilized onto a glutaradehyde (GA) activated NH 2 -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 IC 50 values of 13 and 114 nM, respectively. 2009

Original languageEnglish
Pages (from-to)559-562
Number of pages4
Journalanalytical sciences
Volume25
Issue number4
DOIs
Publication statusPublished - Apr 2009

All Science Journal Classification (ASJC) codes

  • Analytical Chemistry

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