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

Toshiro Matsui, Mayu Shimada, Nozomi Saito, Kiyoshi Matsumoto

Research output: Contribution to journalArticlepeer-review

12 Citations (Scopus)

Abstract

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

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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