Abstract
In one case of 2,8-dihydroxyadenine urolithiasis, reduced adenine phosphoribosyltransferase activity was found. The patient's enzyme had normal affinity for adenine but reduced affinity for substrate phosphoribosyl-pyrophosphate. It was much more stable at 60 degrees C than control. It seems that erythrocyte adenine phosphoribosyltransferase obtained from the patient may be a variant enzyme.
Publication types
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Case Reports
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenine / analogs & derivatives*
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Adenine / analysis
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Adenine Phosphoribosyltransferase / deficiency
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Adenine Phosphoribosyltransferase / genetics*
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Adult
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Erythrocytes / enzymology
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Genetic Variation
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Humans
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Kidney Calculi / analysis*
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Kidney Calculi / genetics
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Male
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Pentosyltransferases / genetics*
Substances
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2,8-dihydroxyadenine
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Pentosyltransferases
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Adenine Phosphoribosyltransferase
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Adenine