期刊
PHYTOTHERAPY RESEARCH
卷 18, 期 6, 页码 475-479出版社
WILEY
DOI: 10.1002/ptr.1456
关键词
tyrosinase inhibitory activity; arbutin; hydroquinone; monophenolase inhibitory activity; poor substrate; reversible inhibition
Arbutin, hydroquinone-O-beta-D-glucopyranoside (1) was found to inhibit the oxidation of L-tyrosine (monophenolase activity) catalyzed by mushroom tyrosinase. However, arbutin itself was oxidized as a monophenol substrate at an extremely slow rate, and this oxidation was accelerated as soon as catalytic amounts (0.01 mM) of L-3,4-dihydroxyphenylalanine (L-DOPA) became available as a cofactor. The result observed was supported by monitoring oxygen consumption. The depigmenting mechanism of arbutin previously reported is supportable if a cofactor is not available in the melanocytes. The combination with L-ascorbic acid is a useful application, particularly when oxygen is limited. Copyright (C) 2004 John Wiley Sons, Ltd.
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