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Research Article Free access | 10.1172/JCI105913

Adenine phosphoribosyltransferase deficiency: a previously undescribed genetic defect in man

William N. Kelley, Robert I. Levy, Frederick M. Rosenbloom, J. Frank Henderson, and J. Edwin Seegmiller

[unk]Section on Human Biochemical Genetics, National Institute of Arthritis and Metabolic Diseases and Laboratory of Molecular Diseases, National Heart Institute, National Institutes of Health, Bethesda, Maryland 20014

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[unk]Section on Human Biochemical Genetics, National Institute of Arthritis and Metabolic Diseases and Laboratory of Molecular Diseases, National Heart Institute, National Institutes of Health, Bethesda, Maryland 20014

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[unk]Section on Human Biochemical Genetics, National Institute of Arthritis and Metabolic Diseases and Laboratory of Molecular Diseases, National Heart Institute, National Institutes of Health, Bethesda, Maryland 20014

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[unk]Section on Human Biochemical Genetics, National Institute of Arthritis and Metabolic Diseases and Laboratory of Molecular Diseases, National Heart Institute, National Institutes of Health, Bethesda, Maryland 20014

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[unk]Section on Human Biochemical Genetics, National Institute of Arthritis and Metabolic Diseases and Laboratory of Molecular Diseases, National Heart Institute, National Institutes of Health, Bethesda, Maryland 20014

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Published October 1, 1968 - More info

Published in Volume 47, Issue 10 on October 1, 1968
J Clin Invest. 1968;47(10):2281–2289. https://doi.org/10.1172/JCI105913.
© 1968 The American Society for Clinical Investigation
Published October 1, 1968 - Version history
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Abstract

A deficiency of adenine phosphoribosyltransferase (A-PRTase) is described in four members in three generations of one family. A-PRTase is coded by an autosome and the mutants described in this report are heterozygotes for this enzyme defect. The level of enzyme activity in these heterozygotes was inappropriately low, ranging from 21 to 37% of normal rather than the expected 50% of normal. Examination of various physical and chemical properties of the A-PRTase obtained from the mutant heterozygotes failed to reveal differences from the normal enzyme. These patients have no discernable abnormality in uric acid production despite the finding that patients with a deficiency of a closely related enzyme, hypoxanthine-guanine phosphoribosyltransferase, invariably produce excessive quantities of uric acid. A relationship of the A-PRTase deficiency to the disturbance in lipoprotein metabolism observed in the propositus has not been firmly established. Possible manifestations of the homozygous form of this enzyme deficiency will require identification of such individuals in the future.

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