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Dawson结构的多金属氧酸盐对酪氨酸酶的抑制作用
引用本文:李莉莉,陈丙年,邓阳阳,谢乐芳,邢蕊,王力.Dawson结构的多金属氧酸盐对酪氨酸酶的抑制作用[J].应用化学,2017,34(1):83-89.
作者姓名:李莉莉  陈丙年  邓阳阳  谢乐芳  邢蕊  王力
作者单位:集美大学食品与生物工程学院 福建 厦门 361021;厦门大学附属中山医院演武分院 福建 厦门 361005
基金项目:国家自然科学基金资助项目(21371072)
摘    要:按文献方法合成了两种Dawson结构的多金属氧酸盐,并对其结构进行紫外光谱和红外光谱分析。以H_6P_2Mo_(18)O_(62)]和H_8P_2Mo_(17)Cr(OH_2)O_(61)](简写为P_2Mo_(18)和P_2Mo_(17)Cr)为效应物,采用紫外分光光度法和酶动力学方法研究两种Dawson结构的多金属氧酸盐效应物对蘑菇酪氨酸酶二酚酶活性的抑制作用。结果表明,P_2Mo_(18)和P_2Mo_(17)Cr对酪氨酸酶二酚酶均具有显著的抑制效果,测定抑制酪氨酸酶活力下降50%的抑制浓度(IC_(50))分别为(0.482±0.009)mmol/L和(0.503±0.011)mmol/L。动力学分析表明,P_2Mo_(18)和P_2Mo_(17)Cr对酪氨酸酶的抑制作用均表现为可逆的竞争型,抑制常数K_I分别为0.212和0.249 mmol/L。其中,综合考虑IC_(50)值和抑制常数,P_2Mo_(18)对酪氨酸酶二酚酶活性的抑制效果略优于P_2Mo_(17)Cr。

关 键 词:酪氨酸酶  抑制剂  多金属氧酸盐  二酚酶活性  
收稿时间:2016-03-07

Inhibitory Effects of Dawson Type Polyoxometalates on Tyrosinase
LI Lili,CHEN Bingnian,DENG Yangyang,XIE Lefang,XING Rui,WANG Li.Inhibitory Effects of Dawson Type Polyoxometalates on Tyrosinase[J].Chinese Journal of Applied Chemistry,2017,34(1):83-89.
Authors:LI Lili  CHEN Bingnian  DENG Yangyang  XIE Lefang  XING Rui  WANG Li
Institution:College of Food and Biological Engineering,Jimei University,Xiamen,Fujian 361021,China;Yanwu Affiliated Hospital of Zhongshan Hospital,Xiamen University,Xiamen,Fujian 361005,China
Abstract:Tyrosinase is a complicated copper containing oxidoreductase that is common in microorganism, plants, animals and human body, which plays a crucial role in melanin biosynthesis. Currently researches about tyrosinase inhibitors are mostly focused on natural extracts and organism. However, inorganic Dawson type polyoxometalates as tyrosinase inhibitors have been less reported. Two kinds of Dawson type polyoxometalates were synthesized and characterized by ultraviolet spectroscopy and infrared spectral analysis. The inhibitory effects of H6P2Mo18O62] and H8P2Mo17Cr(OH2)O61](abbreviated to P2Mo18 and P2Mo17Cr, respectively) on mushroom tyrosinase were investigated by ultraviolet spectrophotometry and enzymatic kinetics methods. P2Mo18 and P2Mo17Cr have significant inhibitory effects on tyrosinase, and the IC50 values of P2Mo18 and P2Mo17Cr are (0.482±0.009) mmol/L and (0.503±0.011) mmol/L for diphenolase, respectively. Enzymatic kinetics analysis indicates that P2Mo18 and P2Mo17Cr are reversible and competitive inhibitor, and the inhibition constant of P2Mo18 and P2Mo17Cr are 0.212 mmol/L and 0.249 mmol/L, respectively. Considering of IC50 values and inhibition constants, the inhibitory effect of P2Mo18 is slightly better than that of P2Mo17Cr. In conclusion, P2Mo18 and P2Mo17Cr show effective antityrosinase activities. Compared with arbutin, P2Mo18 and P2Mo17Cr have much more inhibitory effects on the diphenolase activity of tyrosinase. This study may provide reference foundation for the further study of the tyrosinase inhibitors, and also offer useful information for the comprehensive utilization of polyoxometalates.
Keywords:tyrosinase  inhibitor  polyoxometalates  diphenolase activity
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