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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4308
|
pubmed:dateCreated |
1977-9-29
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pubmed:abstractText |
Erythrocyte purine nucleoside phosphorylase from two brothers had 0.5% of normal activity. It differed from the normal enzyme by a tenfold increase in the Michaelis constant for inosine, an inability of inosine to protect against thermal lability, and a more positive net charge. The altered kinetic properties may account for the milder disease in the patients compared to the previously described cases. The data provide evidence for a structural gene mutation and genetic heterogeneity in the new disease of purine nucleoside phosphorylase deficiency and T cell dysfunction.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Sep
|
pubmed:issn |
0036-8075
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
9
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pubmed:volume |
197
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1084-6
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pubmed:dateRevised |
2007-3-19
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pubmed:meshHeading |
pubmed-meshheading:407651-Child,
pubmed-meshheading:407651-Erythrocytes,
pubmed-meshheading:407651-Humans,
pubmed-meshheading:407651-Hypoxanthines,
pubmed-meshheading:407651-Immune System Diseases,
pubmed-meshheading:407651-Inosine,
pubmed-meshheading:407651-Kinetics,
pubmed-meshheading:407651-Male,
pubmed-meshheading:407651-Mutation,
pubmed-meshheading:407651-Pentosyltransferases,
pubmed-meshheading:407651-Purine-Nucleoside Phosphorylase
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pubmed:year |
1977
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pubmed:articleTitle |
Purine nucleoside phosphorylase deficiency: altered kinetic properties of a mutant enzyme.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.,
Case Reports
|