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Molecules ; 23(10)2018 Oct 22.
Article in English | MEDLINE | ID: mdl-30360380

ABSTRACT

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 (Melilotus albus) 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 IC50 value of 4.13 µM. Further inhibition kinetics data indicated it to be a mixed-type inhibitor and Ki and KI 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.


Subject(s)
Enzyme Inhibitors/pharmacology , Flavonoids/pharmacology , Melilotus/chemistry , Plant Extracts/pharmacology , Xanthine Oxidase/antagonists & inhibitors , Chromatography, High Pressure Liquid , Enzyme Activation/drug effects , Enzyme Inhibitors/chemistry , Enzyme Inhibitors/isolation & purification , Flavonoids/chemistry , Flavonoids/isolation & purification , Models, Molecular , Molecular Conformation , Plant Extracts/chemistry , Protein Binding , Solubility , Structure-Activity Relationship
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