Determining acetylcholinesterase inhibitory activity in plant extracts using a fluorimetric flow assay | Zendy

Rhee In Kyung | Zendy; Appels Natalie | Zendy; Luijendijk Teus | Zendy; Irth Hubertus | Zendy; Verpoorte Robert | Zendy

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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.

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