化学
酪氨酸酶
麦角新碱
IC50型
硫脲
组氨酸
非竞争性抑制
生物化学
立体化学
酶
抗氧化剂
有机化学
体外
作者
Wayne C. Liao,Wen Wu,Pei‐Chuan Tsai,Hui-Feng Wang,Yi‐Hsin Liu,Chin‐Feng Chan
标识
DOI:10.1007/s12010-011-9421-x
摘要
The native amino acid ergothioneine, a thiourea derivative of histidine, inhibits mushroom tyrosinase activity in a dose-dependent manner, with an IC50 value of 1.025 mg/ml (4.47 mM). By contrast, histidine exhibited no inhibitory effect on mushroom tyrosinase activity. We characterized ergothioneine as a noncompetitive tyrosinase inhibitor using a Lineweaver–Burk plot of experimental kinetic data. The IC50 value for ergothioneine scavenging of 2,2-diphenyl-1-picrylhydrazyl was 6.110 ± 0.305 mg/ml, much higher than the IC50 for inhibition of tyrosinase activity which indicating ergothioneine on tyrosinase shows a weak correlation to its antioxidative activity. The results demonstrated that ergothioneine has a potent inhibition effect on tyrosinase enzyme activity, resulting from the presence of the sulfur substituted imidazole ring in ergothioneine.
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