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

Toshiro Matsui, Mayu Shimada, Nozomi Saito, Kiyoshi Matsumoto

研究成果: ジャーナルへの寄稿記事

10 引用 (Scopus)

抄録

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

元の言語英語
ページ(範囲)559-562
ページ数4
ジャーナルanalytical sciences
25
発行部数4
DOI
出版物ステータス出版済み - 4 2009

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Acarbose
Glucosidases
Immobilized Enzymes
Enzyme activity
Fluorescent Dyes
Alanine
Rats
Assays
voglibose

All Science Journal Classification (ASJC) codes

  • Analytical Chemistry

これを引用

α-Glucosidase inhibition assay in an enzyme-immobilized amino-microplate. / Matsui, Toshiro; Shimada, Mayu; Saito, Nozomi; Matsumoto, Kiyoshi.

:: analytical sciences, 巻 25, 番号 4, 04.2009, p. 559-562.

研究成果: ジャーナルへの寄稿記事

Matsui, Toshiro ; Shimada, Mayu ; Saito, Nozomi ; Matsumoto, Kiyoshi. / α-Glucosidase inhibition assay in an enzyme-immobilized amino-microplate. :: analytical sciences. 2009 ; 巻 25, 番号 4. pp. 559-562.
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