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Enzyme Defect in a Case of Xanthinuria

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Abstract

THE enzyme xanthine oxidase which catalyses the oxidation of hypoxanthine to xanthine and of xanthine to uric acid is present in human liver, small-intestinal mucosa and milk1, although the levels of activity appear to be somewhat lower than in animals. Dent and Philpot2 and Dickinson and Smellie3 reported on a patient with xanthine urinary stones, increased urinary oxypurine excretion and very low blood and urine uric acid levels. They suggested that this patient was either unable to oxidize xanthine to uric acid or that there was a failure of xanthine reabsorption by the renal tubules, or that both these defects were present.

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Authors and Affiliations

  1. Arthritis and Rheumatism Branch, National Institute of Arthritis and Metabolic Diseases and Experimental Therapeutics Branch, National Heart Institute, National Institutes of Health, Bethesda, Md

    RICHARD W. E. WATTS, KARL ENGELMAN, JAMES R. KLINENBERG, J. EDWIN SEEGMILLER & ALBERT SJOERDSMA

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  1. RICHARD W. E. WATTS
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  2. KARL ENGELMAN
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  3. JAMES R. KLINENBERG
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  4. J. EDWIN SEEGMILLER
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  5. ALBERT SJOERDSMA
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WATTS, R., ENGELMAN, K., KLINENBERG, J. et al. Enzyme Defect in a Case of Xanthinuria. Nature 201, 395–396 (1964). https://doi.org/10.1038/201395a0

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