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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1990-5-23
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pubmed:abstractText |
Genetic heterogeneity has been suggested in xanthinuria from the hitherto unexplained ability of some patients with this hereditary disorder to convert allopurinol to its active metabolite oxipurinol--an activity generally attributed to xanthine oxidase. This study provides evidence that the enzyme aldehyde oxidase is also deficient in xanthinuric patients not converting allopurinol to oxipurinol, whereas a xanthinuric patient with normal formation of oxipurinol had normal aldehyde oxidase activity. It is concluded that the enzyme aldehyde oxidase is the principal enzyme responsible for the formation of oxipurinol in man.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
|
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0009-8981
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pubmed:author |
|
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
187
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
221-34
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:2323062-Adult,
pubmed-meshheading:2323062-Aldehyde Oxidase,
pubmed-meshheading:2323062-Aldehyde Oxidoreductases,
pubmed-meshheading:2323062-Allopurinol,
pubmed-meshheading:2323062-Humans,
pubmed-meshheading:2323062-Male,
pubmed-meshheading:2323062-Middle Aged,
pubmed-meshheading:2323062-Oxypurinol,
pubmed-meshheading:2323062-Purine-Pyrimidine Metabolism, Inborn Errors,
pubmed-meshheading:2323062-Pyrimidines,
pubmed-meshheading:2323062-Xanthine Oxidase,
pubmed-meshheading:2323062-Xanthines
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pubmed:year |
1990
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pubmed:articleTitle |
Demonstration of a combined deficiency of xanthine oxidase and aldehyde oxidase in xanthinuric patients not forming oxipurinol.
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pubmed:affiliation |
Medizinische Poliklinik, Klinikum Grosshadern, Universität München, FRG.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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