Results 211 to 220 of about 12,040 (235)
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Tyrosinase Inhibitors from Cumin
Journal of Agricultural and Food Chemistry, 1998Cuminaldehyde (p-isopropylbenzaldehyde) was identified as a potent mushroom tyrosinase inhibitor from cumin, a common food spice. This benzaldehyde derivative was found to inhibit the oxidation of l-3,4-dihydroxyphenylalanine (l-DOPA) by mushroom tyrosinase with an ID50 of 7.7 μg/mL (0.05 mM). Its oxidized analogue, cumic acid (p-isopropylbenzoic acid),
Isao Kubo, Ikuyo Kinst-Hori
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Tyrosinase Inhibitor from Black Rice Bran
Journal of Agricultural and Food Chemistry, 2003The inhibitor of tyrosinase activity in black rice bran was investigated. The methanol extract from black rice bran was re-extracted with hexane, chloroform, ethyl acetate, or water. The ethyl acetate extract had the most potent inhibition against tyrosinase activity by 80.5% at a concentration of 0.4 mg/mL.
Mitsuo, Miyazawa +4 more
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Activity regulation of tyrosinase by using photoisomerizable inhibitors
Journal of Biotechnology, 2004Enzymatic activity of tyrosinase was controlled on the basis of cis-trans photoisomerization of inhibitors, 4-azobenzene carboxylic acid (ACA) and 4,4'-azobenzene dicarboxylic acid (ADCA). In the case of ACA, the cis form inhibited tyrosinase-catalyzed oxidation of L-tyrosine more strongly than the trans form.
Kikuo, Komori +2 more
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Functionality study of Na6PMo11FeO40 as a mushroom tyrosinase inhibitor
Food Chemistry, 2015The inhibitory effects of iron-substituted phosphomolybdic acid (Na6PMo11FeO40, abbreviated as PMo11Fe) on mushroom tyrosinase were investigated. The Native-PAGE results show that PMo11Fe has an inhibitory effect on tyrosinase. A spectrophotometric analysis shows that PMo11Fe is a reversible and noncompetitive inhibitor with KI=KIS=0.47 mmol L(-1). The
Rui, Xing +5 more
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Tyrosinase Inhibitors from Terrestrial and Marine Resources
Current Topics in Medicinal Chemistry, 2014Tyrosinase is a multifunctional copper-containing enzyme widely distributed in plants and animals, which catalyzes both the hydroxylation of tyrosine into o-diphenols and the oxidation of o-diphenols into o-quinones. Tyrosinase is known to be a key enzyme for melanin biosynthesis in plants and animals.
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Tyrosinase inhibition by its apoenzyme and the transformation of a protein inhibitor into tyrosinase
Biochemical and Biophysical Research Communications, 1961Y, KARKHANIS, E, FRIEDEN
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Rifampicin as a novel tyrosinase inhibitor: Inhibitory activity and mechanism
International Journal of Biological Macromolecules, 2017Wei-Ming Chai +2 more
exaly
L-mimosine a slow-binding inhibitor of mushroom tyrosinase
Phytochemistry, 1987J Cabanes +2 more
exaly