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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
19
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pubmed:dateCreated |
1983-11-23
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pubmed:abstractText |
The size of the Ca2+ pump protein in canine cardiac sarcoplasmic reticulum (SR) membranes was determined using target theory analysis of radiation-inactivation data. Samples of cardiac SR were irradiated in the frozen state with increasing doses of high energy electrons from a Van de Graaff accelerator. The loss of Ca2+-dependent ATPase activity and of ATP-dependent, oxalate-facilitated Ca2+ uptake (loading) with increasing irradiation dosage paralleled one another. Also, the loss of staining intensity of the predominant polypeptide (Mr = 110,000) in sodium dodecyl sulfate-polyacrylamide gel electrophoresis correlated with the loss of ATPase and loading activities. The target size by all three measurements varied between 213,000 and 229,000 Da. We conclude that the Ca2+ pump protein in canine cardiac SR is a dimer.
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pubmed:grant | |
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 |
Oct
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
258
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
11997-2001
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:6225783-Animals,
pubmed-meshheading:6225783-Calcium-Transporting ATPases,
pubmed-meshheading:6225783-Dogs,
pubmed-meshheading:6225783-Dose-Response Relationship, Radiation,
pubmed-meshheading:6225783-Macromolecular Substances,
pubmed-meshheading:6225783-Methods,
pubmed-meshheading:6225783-Molecular Weight,
pubmed-meshheading:6225783-Myocardium,
pubmed-meshheading:6225783-Sarcoplasmic Reticulum
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pubmed:year |
1983
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pubmed:articleTitle |
Determination of the oligomeric structure of the Ca2+ pump protein in canine cardiac sarcoplasmic reticulum membranes using radiation inactivation 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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