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Determining acetylcholinesterase inhibitory activity in plant extracts using a fluorimetric flow assay
Author(s) -
Rhee In Kyung,
Appels Natalie,
Luijendijk Teus,
Irth Hubertus,
Verpoorte Robert
Publication year - 2003
Publication title -
phytochemical analysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.574
H-Index - 72
eISSN - 1099-1565
pISSN - 0958-0344
DOI - 10.1002/pca.695
Subject(s) - chemistry , acetylcholinesterase , chromatography , substrate (aquarium) , aché , inhibitory postsynaptic potential , iodide , detection limit , hydrolysis , amaryllidaceae , enzyme , methanol , biochemistry , organic chemistry , botany , oceanography , neuroscience , biology , geology
A fluorometric assay for acetylcholinesterase inhibitory activity was developed in a flow system using the fluorogenic substrate 7‐acetoxy‐1‐methyl quinolinium iodide which is hydrolysed to the highly fluorescent 7‐hydroxy‐1‐methyl quinolinium iodide. The detection limit of galanthamine is 0.5 µ M , which is about 20 times more sensitive than in the colorimetric flow assay. In the presence of 30% methanol or of 5% acetonitrile, about 70% of the enzyme activity could still be detected. Various plant extracts have been screened using the described system including bulbs of Galanthus nivalis, Eucharis amazonica ( E . × grandiflora ), Crinum powelli and Nerine bowdenii (all members of the Amaryllidaceae), which showed strong AchE inhibitory activity. Copyright © 2003 John Wiley & Sons, Ltd.