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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
10
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pubmed:dateCreated |
1990-3-2
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pubmed:abstractText |
The relationships between cholesterol 7 alpha-hydroxylase activity, pool of free microsomal cholesterol, and degree of substrate saturation of the enzyme were studied in untreated (n = 5), cholesterol-fed (n = 4), and cholestyramine-treated (n = 6) gallstone patients undergoing cholecystectomy. Highly accurate methods based on isotope dilution-mass spectrometry were used for assay of the cholesterol 7 alpha-hydroxylase activity and for determination of the concentration of free cholesterol in the microsomes. The cholesterol-enriched diet increased the cholesterol 7 alpha-hydroxylase activity about twofold. Cholestyramine treatment was associated with a five- to sixfold increase of the cholesterol 7 alpha-hydroxylase activity. The concentration of free microsomal cholesterol remained essentially unchanged. The apparent degree of saturation of the enzyme was calculated to be 85% in the untreated patients, 86% in the cholesterol-fed patients, and 67% in those treated with cholestyramine. A significant negative correlation was obtained between enzyme activity and apparent substrate saturation. It is concluded that the apparent substrate saturation of the cholesterol 7 alpha-hydroxylase in human liver microsomes is high but that availability of cholesterol may limit the enzyme activity to some extent a high bile acid synthesis rates.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bile Acids and Salts,
http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol, Dietary,
http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol 7-alpha-Hydroxylase,
http://linkedlifedata.com/resource/pubmed/chemical/Cholestyramine Resin,
http://linkedlifedata.com/resource/pubmed/chemical/Steroid Hydroxylases
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0022-2275
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
30
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1477-81
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:2614251-Adult,
pubmed-meshheading:2614251-Aged,
pubmed-meshheading:2614251-Bile Acids and Salts,
pubmed-meshheading:2614251-Cholelithiasis,
pubmed-meshheading:2614251-Cholesterol, Dietary,
pubmed-meshheading:2614251-Cholesterol 7-alpha-Hydroxylase,
pubmed-meshheading:2614251-Cholestyramine Resin,
pubmed-meshheading:2614251-Female,
pubmed-meshheading:2614251-Humans,
pubmed-meshheading:2614251-Male,
pubmed-meshheading:2614251-Microsomes, Liver,
pubmed-meshheading:2614251-Middle Aged,
pubmed-meshheading:2614251-Steroid Hydroxylases
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pubmed:year |
1989
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pubmed:articleTitle |
On the saturation of the cholesterol 7 alpha-hydroxylase in human liver microsomes.
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pubmed:affiliation |
Department of Medicine, Karolinska Institute, Huddinge University Hospital, Sweden.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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