Fluorometric Rate Assay of α-Amylase Using an Intramolecularly-Quenched Fluorescent Substrate (FG5P)

抄録

The complete hydrolysis of a fluorogenic derivative of p-nitrophenyl α-maltopentaoside, FG5P, by human salivary α-amylase, resulted in a 5-fold increase in fluorescence. This is due to disruption of the intramolecular quenching of the fluorescence of the 2-pyridylamino residue by the p-nitrophenyl residue by separation of the two residues. This change of fluorescence accompanying the cleavage of the glucosidic bond was exploited to develop a fluorometric rate assay of α-amylase in human serum.