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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1994-11-10
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pubmed:abstractText |
Myotoxin alpha from prairie rattlesnakes induced Ca2+ release from the heavy fraction of sarcoplasmic reticulum at submicromolar concentrations. 125I-Labeled myotoxin alpha (125I-myotoxin alpha) specifically bound to the heavy fraction. Fractionation of the solubilized heavy fraction with a spermine-agarose column gave purified calsequestrin as a major binding protein of 125I-myotoxin alpha. We have first indicated that calsequestrin is a target protein for Ca(2+)-releasing action of myotoxin alpha. Calsequestrin probably plays a key role in physiological Ca2+ release from sarcoplasmic reticulum.
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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 |
Jun
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pubmed:issn |
0014-2999
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
268
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
R1-2
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pubmed:dateRevised |
2003-11-14
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pubmed:meshHeading | |
pubmed:year |
1994
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pubmed:articleTitle |
Calsequestrin is a major binding protein of myotoxin alpha and an endogenous Ca2+ releaser in sarcoplasmic reticulum.
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pubmed:affiliation |
Department of Pharmaceutical Molecular Biology, Tohoku University, Sendai, Japan.
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pubmed:publicationType |
Journal Article
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