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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1988-8-11
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pubmed:abstractText |
Upon tryptic digestion of synaptosomes, ATPase activities decreased in the order of Cl(-)-ATPase greater than or equal to Na+,K+-ATPase greater than anion-insensitive Mg2+-ATPase. Upon synaptosome treatment with hypotonic solution, Cl(-)-ATPase or anion-insensitive Mg2+-ATPase was slightly inactivated, while Na+,K+-ATPase underwent a much larger degree of inactivation. ATP-Mg inhibited the ATPase digestion in the hypotonic-solution-treated synaptosomes in a concentration-dependent manner, but not in the untreated synaptosomes. These results suggest that trypsin-digestible site of Cl(-)-ATPase are present on both sides of the synaptosomal plasma membrane, and the ATP-Mg binding site of the enzyme is located on the inner surface of the membrane.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Anion Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium-Potassium-Exchanging ATPase,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin,
http://linkedlifedata.com/resource/pubmed/chemical/anion-sensitive ATPases
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0386-7196
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
13
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
105-11
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:2838180-Adenosine Triphosphatases,
pubmed-meshheading:2838180-Animals,
pubmed-meshheading:2838180-Anion Transport Proteins,
pubmed-meshheading:2838180-Brain,
pubmed-meshheading:2838180-Rats,
pubmed-meshheading:2838180-Sodium-Potassium-Exchanging ATPase,
pubmed-meshheading:2838180-Synaptosomes,
pubmed-meshheading:2838180-Trypsin
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pubmed:year |
1988
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pubmed:articleTitle |
Proteolytic digestion of Cl(-)-ATPase in rat brain synaptosomes.
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pubmed:affiliation |
Department of Biology, Kyoto Pharmaceutical University, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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