Inhibition of xanthine oxidase by liquiritigenin and isoliquiritigenin isolated from Sinofranchetia chinensis

Cell Mol Life Sci. 2000 Mar;57(3):500-5. doi: 10.1007/PL00000710.

Abstract

The methanol extract of the stem of Sinofranchetia inhibited the activity of xanthine oxidase in vitro. Bioassay-guided purification led to the isolation ofliquiritigenin and isoliquiritigenin as the main xanthine oxidase inhibitors. This inhibition of enzyme activity was found to be dose dependent, with an IC50 value of approximately 49.3 microM for liquiritigenin and 55.8 microM for isoliquiritigenin. Lineweaver-Burk transformation of the inhibition data indicated that the inhibition was of a mixed type for both liquiritigenin and isoliquiritigenin. For liquiritigenin, the Ki and K(I) were determined to be 14.0 microM and 151.6 microM, respectively. For isoliquiritigenin, the Ki and K(I) were determined to be 17.4 microM and 81.9 microM, respectively. These results suggest that these natural products could be used to treat conditions where the inhibition of xanthine oxidase is warranted.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cattle
  • Chalcone / analogs & derivatives*
  • Chalcone / isolation & purification
  • Chalcone / pharmacology
  • Chalcones
  • Enzyme Inhibitors / isolation & purification
  • Enzyme Inhibitors / pharmacology*
  • Flavanones
  • Flavonoids / isolation & purification
  • Flavonoids / pharmacology*
  • Hypolipidemic Agents / isolation & purification
  • Hypolipidemic Agents / pharmacology*
  • Phytotherapy
  • Plants, Medicinal*
  • Xanthine Oxidase / antagonists & inhibitors*

Substances

  • Chalcones
  • Enzyme Inhibitors
  • Flavanones
  • Flavonoids
  • Hypolipidemic Agents
  • Chalcone
  • isoliquiritigenin
  • Xanthine Oxidase
  • liquiritigenin