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rdf:type |
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lifeskim:mentions |
umls-concept:C0001044,
umls-concept:C0006104,
umls-concept:C0013139,
umls-concept:C0020045,
umls-concept:C0025255,
umls-concept:C0031671,
umls-concept:C0205227,
umls-concept:C0208973,
umls-concept:C0332324,
umls-concept:C1517892,
umls-concept:C1704666
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pubmed:issue |
4
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pubmed:dateCreated |
1988-4-21
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pubmed:abstractText |
The sensitivity of acetylcholinesterases (AChEs) from Musca domestica and from Drosophila melanogaster to the phosphatidylinositol-specific phospholipase C from Bacillus cereus and to the glycosylphosphatidylinositol-specific phospholipase C from Trypanosoma brucei was investigated. B. cereus phospholipase C solubilizes membrane-bound AChE, and both phospholipases convert amphiphilic AChEs into hydrophilic forms of the enzyme. The lipases uncover an immunological determinant that is found on other glycosylphosphatidylinositol-anchored membrane proteins after the same treatment. This immunological determinant is also present on the native hydrophilic form of AChE. The polypeptide bearing the active site of the membrane-bound enzyme migrates faster during sodium dodecyl sulfate-polyacrylamide gel electrophoresis than the same polypeptide from the soluble enzyme. We conclude that AChE from insect brain is attached to membranes via a glycophospholipid anchor. This anchor is covalently linked to the polypeptide bearing the active esterase site of the enzyme and can be cleaved by an endogenous lipase.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acetylcholinesterase,
http://linkedlifedata.com/resource/pubmed/chemical/Glycosylphosphatidylinositol...,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Lipids,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol...,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositols,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoinositide Phospholipase C,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoric Diester Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Type C Phospholipases
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0022-3042
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
50
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1158-63
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pubmed:dateRevised |
2007-11-19
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pubmed:meshHeading |
pubmed-meshheading:2831298-Acetylcholinesterase,
pubmed-meshheading:2831298-Animals,
pubmed-meshheading:2831298-Bacillus cereus,
pubmed-meshheading:2831298-Brain,
pubmed-meshheading:2831298-Cell Membrane,
pubmed-meshheading:2831298-Drosophila melanogaster,
pubmed-meshheading:2831298-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:2831298-Glycosylphosphatidylinositol Diacylglycerol-Lyase,
pubmed-meshheading:2831298-Houseflies,
pubmed-meshheading:2831298-Immunoassay,
pubmed-meshheading:2831298-Kinetics,
pubmed-meshheading:2831298-Macromolecular Substances,
pubmed-meshheading:2831298-Membrane Lipids,
pubmed-meshheading:2831298-Membrane Proteins,
pubmed-meshheading:2831298-Phosphatidylinositol Diacylglycerol-Lyase,
pubmed-meshheading:2831298-Phosphatidylinositols,
pubmed-meshheading:2831298-Phosphoinositide Phospholipase C,
pubmed-meshheading:2831298-Phospholipases,
pubmed-meshheading:2831298-Phosphoric Diester Hydrolases,
pubmed-meshheading:2831298-Solubility,
pubmed-meshheading:2831298-Trypanosoma brucei brucei,
pubmed-meshheading:2831298-Type C Phospholipases
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pubmed:year |
1988
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pubmed:articleTitle |
Acetylcholinesterases from Musca domestica and Drosophila melanogaster brain are linked to membranes by a glycophospholipid anchor sensitive to an endogenous phospholipase.
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pubmed:affiliation |
INRA, Centre de Recherche d'Antibes, France.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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