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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3-4
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pubmed:dateCreated |
1987-4-3
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pubmed:abstractText |
We have previously identified N-acylethanolamine phospholipids in infarcted dog heart and in normal fish brain by chemical and enzymatic degradation. We now report that hydrolysis with phospholipase D from Streptomyces chromofuscus removes N-acylethanolamine from N-acylethanolamine phospholipids and lyso N-acylethanolamine phospholipids, or N-acylserine from lyso N-acylserine phospholipids. At acidic pH, a phosphatase present in the phospholipase D preparation further hydrolyzes the resulting phosphatidic acid (PA) or lyso-PA to diacyl- or monoacylglycerol. Because N-acylserine phospholipids are a poor substrate for the phospholipase D, pretreatment with phospholipase A2 (Trimeresurus flavoviridis venom) is used to remove the 2-O-acyl group. Thus, both types of N-acylated phospholipids can be analyzed by consecutive phospholipase A2 and phospholipase D treatment. Reaction products, i.e., free fatty acids, monoacylglycerols and N-acylethanolamine or N-acylserine, are separable by thin-layer chromatography. Both N-acyl components can be further characterized by conversion to the t-butyldimethylsilyl derivatives. The method was used to identify and analyze the N-acylserine phospholipids of bovine brain.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acids, Nonesterified,
http://linkedlifedata.com/resource/pubmed/chemical/Glycerophosphates,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipase D,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipases,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipases A,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipases A2,
http://linkedlifedata.com/resource/pubmed/chemical/Snake Venoms
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pubmed:status |
MEDLINE
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pubmed:issn |
0009-3084
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
41
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
195-207
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:3815621-Acylation,
pubmed-meshheading:3815621-Animals,
pubmed-meshheading:3815621-Fatty Acids, Nonesterified,
pubmed-meshheading:3815621-Glycerophosphates,
pubmed-meshheading:3815621-Hydrolysis,
pubmed-meshheading:3815621-Phospholipase D,
pubmed-meshheading:3815621-Phospholipases,
pubmed-meshheading:3815621-Phospholipases A,
pubmed-meshheading:3815621-Phospholipases A2,
pubmed-meshheading:3815621-Snake Venoms,
pubmed-meshheading:3815621-Streptomyces,
pubmed-meshheading:3815621-Substrate Specificity
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pubmed:articleTitle |
Hydrolysis of N-acylated glycerophospholipids by phospholipases A2 and D: a method of identification and analysis.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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