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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
1997-5-22
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pubmed:abstractText |
Phospholipase D of rat brain synaptosomal membranes was tested with phosphatidylcholine as the substrate for its specificity in the use of primary alcohols as transphosphatidylation co-substrates. The efficiency of the reaction was related to the hydrophobicity and the membrane penetrating capacity of the alcohol molecule. Phosphatidylalcohol formation could be detected up to 1-octanol but not for alcohols with longer hydrocarbon chains (C(9), C(10)). With increasing alcohol concentration the transphosphatidylation activity of the phospholipase D reached an optimum and then declined abruptly. Alcohol concentrations required for maximal transphosphatidylation reaction generally decreased with increasing hydrophobicities of the alcohols. Nevertheless 1-butanol and 4-chloro-1-butanol were the most efficient cosubstrates, sharing identical optimal conditions. Transphosphatidylation works at the cost of phosphatidic acid formation. Phosphatidic acid itself was transformed to diacylglycerol, probably by a contaminating phosphatidic acid phosphohydrolase.
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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 |
Apr
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pubmed:issn |
0901-9928
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
78
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
249-53
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:8861783-Alcohols,
pubmed-meshheading:8861783-Animals,
pubmed-meshheading:8861783-Brain,
pubmed-meshheading:8861783-Chemistry, Physical,
pubmed-meshheading:8861783-Membranes,
pubmed-meshheading:8861783-Phosphatidylcholines,
pubmed-meshheading:8861783-Phospholipase D,
pubmed-meshheading:8861783-Physicochemical Phenomena,
pubmed-meshheading:8861783-Rats,
pubmed-meshheading:8861783-Synaptosomes
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pubmed:year |
1996
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pubmed:articleTitle |
Primary alcohols and phosphatidylcholine metabolism in rat brain synaptosomal membranes via phospholipase D.
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pubmed:affiliation |
Division of Pathochemistry, German Cancer Research Center, Heidelberg, Germany.
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pubmed:publicationType |
Journal Article,
In Vitro
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