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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
|
pubmed:dateCreated |
1989-1-27
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pubmed:abstractText |
C27-steroid 26-hydroxylase activity in fibroblasts from two heterozygotes for CTX was determined, using an optimized enzyme assay. With 5 beta-cholestane-3 alpha,7 alpha,12 alpha-triol, 5 beta-cholestane-3 alpha,7 alpha-diol, 7 alpha-hydroxy-4-cholestane-3-one or 7 alpha-hydroxycholesterol as substrates, the activities were about 50% of those of control cells. The Km for the substrates was not increased in the CTX heterozygotes. These findings support that deficiency of the C27-steroid 26-hydroxylase is the primary enzymatic defect in CTX.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:status |
MEDLINE
|
pubmed:month |
Sep
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pubmed:issn |
0036-5513
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
48
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
425-9
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:3206189-Adult,
pubmed-meshheading:3206189-Brain Diseases,
pubmed-meshheading:3206189-Cells, Cultured,
pubmed-meshheading:3206189-Female,
pubmed-meshheading:3206189-Heterozygote,
pubmed-meshheading:3206189-Humans,
pubmed-meshheading:3206189-Male,
pubmed-meshheading:3206189-Tendons,
pubmed-meshheading:3206189-Xanthomatosis
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pubmed:year |
1988
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pubmed:articleTitle |
Reduced C27-steroid 26-hydroxylase activity in heterozygotes for cerebrotendinous xanthomatosis.
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pubmed:affiliation |
Institute of Clinical Biochemistry, University of Oslo, Rikshospitalet, Norway.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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