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

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Abstract.

The methanol extract of the stem of Sinofranchetia chinensis inhibited the activity of xanthine oxidase in vitro. Bioassay-guided purification led to the isolation of liquiritigenin 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 μM for liquiritigenin and 55.8 μM 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 KI were determined to be 14.0 μM and 151.6 μM, respectively. For isoliquiritigenin, the Ki and KI were determined to be 17.4 μM and 81.9 μM, respectively. These results suggest that these natural products could be used to treat conditions where the inhibition of xanthine oxidase is warranted.

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Authors and Affiliations

  1. State Key Laboratory of Pharmaceutical Biotechnology, Institute of Pharmaceutical Biology and Phytochemistry, Nanjing University, Nanjing 210093 (China), , , , , , CN

    L. D. Kong, Y. Zhang & R. X. Tan

  2. Department of Biochemistry, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong (China), Fax +852 2603 5123, e-mail: chkcheng@cuhk.edu.hk, , , , , , CN

    C. H. K. Cheng*

  3. Department of Pharmacy, Lanzhou Medical College, Lanzhou 730000 (China), , , , , , CN

    X. Pan

Authors
  1. L. D. Kong
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  2. Y. Zhang
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  3. X. Pan
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  4. R. X. Tan
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  5. C. H. K. Cheng*
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Additional information

Received 6 October 1999; received after revision 3 December 1999; accepted 4 January 2000

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Kong, L., Zhang, Y., Pan, X. et al. Inhibition of xanthine oxidase by liquiritigenin and isoliquiritigenin isolated from Sinofranchetia chinensis. CMLS, Cell. Mol. Life Sci. 57, 500–505 (2000). https://doi.org/10.1007/PL00000710

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  • DOI: https://doi.org/10.1007/PL00000710

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