Isolation of Tricin as a Xanthine Oxidase Inhibitor from Sweet White Clover ( Melilotus albus ) and Its Distribution in Selected Gramineae Species

Xanthine oxidase, an enzyme present in significant levels in the intestine and liver, metabolizes hypoxanthine to xanthine and xanthine to uric acid in the purine catabolic pathway. An inhibitory compound acting against xanthine oxidase was isolated from sweet white clover ( ) by bioassay and high-p...

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Published inMolecules (Basel, Switzerland) Vol. 23; no. 10; p. 2719
Main Authors Liu, Xiao-Xiao, Sun, Shi-Wei, Yuan, Wen-Jing, Gao, Hua, Si, Yue-Yue, Liu, Kun, Zhang, Shuang, Liu, Yang, Wang, Wei
Format Journal Article
LanguageEnglish
Published Switzerland MDPI AG 22.10.2018
MDPI
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Summary:Xanthine oxidase, an enzyme present in significant levels in the intestine and liver, metabolizes hypoxanthine to xanthine and xanthine to uric acid in the purine catabolic pathway. An inhibitory compound acting against xanthine oxidase was isolated from sweet white clover ( ) by bioassay and high-performance liquid chromatography guided separation. It was identified as tricin by spectroscopic analysis. Tricin possessed a potent xanthine oxidase inhibitory activity with an IC value of 4.13 μM. Further inhibition kinetics data indicated it to be a mixed-type inhibitor and and values were determined to be 0.47 μM and 4.41 μM. To find a rich source of tricin, the distribution of tricin in seven different tissues from four Gramineae species was investigated by high-performance liquid chromatography analysis. The highest amount (1925.05 mg/kg dry materials) was found in the straw of wheat, which is considered as a potentially valuable source of natural tricin.
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content type line 23
ISSN:1420-3049
1420-3049
DOI:10.3390/molecules23102719