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Publications (2)2.79 Total impact

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    ABSTRACT: Alpha-glucosidase (AGH) from the small intestine of rat was immobilized onto a glutaraldehyde (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 beta-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 degrees C for 2 h using 0.3 mM 4-methylumbelliferyl-alpha-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.
    No preview · Article · May 2009 · Analytical Sciences
  • [Show abstract] [Hide abstract]
    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
    No preview · Article · Apr 2009 · Analytical Sciences