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Chemical and Pharmaceutical Bulletin
Vol. 51 (2003) No. 4 P 409-411




The inhibitory compound of monoamine oxidase (MAO) activity was isolated from the CH2Cl2 fraction of the fructus of Evodia rutaecarpa and identified as 1-methyl-2-undecyl-4(1H)-quinolone (1). Compound 1 showed a selective inhibition of type B MAO (MAO-B) activity with the IC50 value of 15.3 μM using a substrate kynuramine, but did not inhibit type A MAO (MAO-A) activity. The kinetic analysis using Lineweaver-Burk plots indicated that compound 1 competitively inhibited MAO-B activity with the Ki value of 9.91 μM. The inhibition of MAO-B by compound 1 was found to be irreversible by dialysis of the incubation mixture. These results suggest that compound 1 is a potent irreversible inhibitor of MAO-B, and may regulate catecholamine content in the neurons.

Copyright © 2003 The Pharmaceutical Society of Japan

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