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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1977-3-31
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pubmed:abstractText |
The preferential cellular distribution in the villus tip and the subcellular localization in the endoplasmic reticulum of an intestinal glycerol-ester hydrolase from rat mucosa are described. The enzyme is shown not to be from either pancreatic or bacterial origin; it catalyzes the hydrolysis of short- and medium chain triglycerides and of p-nitrophenylacetate. Contrarily to the specificity found for the pig intestinal lipase (Serrero, Négrel and Ailhaud, 1975), no activity is detectable against acylCoA; a thiolester hydrolase different from the glycerol-ester hydrolase was demonstrated after differential solubilization and chromatographic separation. A high proportion of glycerol-ester hydrolase is present in the intestinal lumen; its possible complementary role in lipid degradation is discussed.
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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 |
Dec
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
71
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
249-58
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pubmed:dateRevised |
2009-10-27
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pubmed:meshHeading |
pubmed-meshheading:12956-Aging,
pubmed-meshheading:12956-Animals,
pubmed-meshheading:12956-Glycerides,
pubmed-meshheading:12956-Hydrogen-Ion Concentration,
pubmed-meshheading:12956-Intestinal Mucosa,
pubmed-meshheading:12956-Lipase,
pubmed-meshheading:12956-Male,
pubmed-meshheading:12956-Polyethylene Glycols,
pubmed-meshheading:12956-Precipitin Tests,
pubmed-meshheading:12956-Rats,
pubmed-meshheading:12956-Solubility,
pubmed-meshheading:12956-Subcellular Fractions,
pubmed-meshheading:12956-Surface-Active Agents
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pubmed:year |
1976
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pubmed:articleTitle |
Esterolytic activities of rat intestinal mucosa. 1. Characterization, cellular distribution and subcellular localization of a glycerol-ester hydrolase.
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pubmed:publicationType |
Journal Article
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