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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
1979-11-28
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pubmed:abstractText |
Glycerophosphatides, specifically labeled either in the 1 or in the 2 position, were used to measure the activity of neuronal phospholipase A1 and to investigate the subcellular distribution of the enzyme. The microsomes were found to possess the highest phospholipase activity, with a threefold increase as compared to the cell homogenate. A considerable enzymatic activity could still be observed in the plasma membranes isolated from the neuronal-enriched cell fraction. Microsomal phospholipase possessed the highest activity with phosphatidylcholine, whereas phosphatidylserine was cleaved at a much lower rate. The rate of release of labeled fatty acids from the substrates by the microsomal phospholipase decreased with increasing degree of unsaturation of the fatty acids at the 1 position. The presence of plasmalogens and of alkylacyl analogues in the incubation mixture caused an appreciable inhibition of the hydrolysis of the diacyl glycerophosphatides.
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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 |
Aug
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pubmed:issn |
0364-3190
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
535-43
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:481684-Animals,
pubmed-meshheading:481684-Cerebral Cortex,
pubmed-meshheading:481684-Fatty Acids,
pubmed-meshheading:481684-Neurons,
pubmed-meshheading:481684-Phospholipases,
pubmed-meshheading:481684-Phospholipases A,
pubmed-meshheading:481684-Phospholipases A1,
pubmed-meshheading:481684-Rabbits,
pubmed-meshheading:481684-Subcellular Fractions,
pubmed-meshheading:481684-Substrate Specificity
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pubmed:year |
1979
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pubmed:articleTitle |
Activity and subcellular distribution of phospholipase A1 from neuronal cell-enriched fractions of the rabbit cerebral cortex.
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pubmed:publicationType |
Journal Article
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