Inhibition of xanthine oxidase by purpurogallin and silymarin group

Shiow Yunn Sheu, Chih Hao Lai, Hsüch Ching Chiang

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34 Citations (Scopus)


Thirteen phenolic compounds were tested for their inhibitory effects on xanthine oxidase. The enzyme xanthine oxidase catalyses the oxidation of hypoxanthine to xanthine and of xanthine to uric acid which has λmax of 295 nm, forming the basis for a spectrophotometric assay of the activity of xanthine oxidase. The results showed that purpurogallin and silymarin group displayed the inhibitory effects on xanthine oxidase (IC50 = 2.96 ± 0.12 and 27.58 ± 3.48 μM, respectively). Their apparent inhibition constants (Ki) were 1.16 and 5.85 μM, and induced uncompetitive and mixed type (non-competitive-uncompetitive) inhibitions respectively with respect to the substrate xanthine.

Original languageEnglish
Pages (from-to)263-267
Number of pages5
JournalAnticancer Research
Issue number1 A
Publication statusPublished - Jan 1998


  • Antihepatotoxic principle
  • Antitumor
  • Phenolic compounds
  • Purpurogallin
  • Silymarin group
  • Xanthine oxidase inhibitors

ASJC Scopus subject areas

  • Oncology
  • Cancer Research


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