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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
8
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pubmed:dateCreated |
1989-4-25
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pubmed:abstractText |
Calsequestrin is a high capacity low affinity Ca2+-binding protein thought to be essential for the function of the intracellular rapid releasable Ca2+ pool of a variety of animal cells. Here we show that two types of plant tissues, cultured Streptanthus tortuosus cells and spinach leaves, contain a form of calsequestrin. In subcellular fractions of S. tortuosus cells, Stains-all staining reveals a metachromatically blue-staining 56,000-Da protein enriched in the microsomal fraction. This protein shares several biochemical characteristics with animal calsequestrin: 1) it changes its apparent molecular weight with the pH; 2) it is able to bind 45Ca2+ on nitrocellulose transfers; and 3) it is recognized by antibodies against canine cardiac calsequestrin. Calsequestrin was also identified in spinach leaves using a direct extraction procedure that was developed for muscle calsequestrin. Thus, our results demonstrate that plant cells contain calsequestrin within a subcellular membrane fraction. These results also suggest that calsequestrin is an ubiquitous protein rather than being limited only to animal cells.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Mar
|
pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
15
|
pubmed:volume |
264
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
4269-72
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2925646-Animals,
pubmed-meshheading:2925646-Calcium,
pubmed-meshheading:2925646-Calsequestrin,
pubmed-meshheading:2925646-Dogs,
pubmed-meshheading:2925646-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:2925646-Hydrogen-Ion Concentration,
pubmed-meshheading:2925646-Immunoblotting,
pubmed-meshheading:2925646-Microscopy, Electron,
pubmed-meshheading:2925646-Microsomes,
pubmed-meshheading:2925646-Molecular Weight,
pubmed-meshheading:2925646-Muscle Proteins,
pubmed-meshheading:2925646-Myocardium,
pubmed-meshheading:2925646-Plants
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pubmed:year |
1989
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pubmed:articleTitle |
Plant cells contain calsequestrin.
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pubmed:affiliation |
Department of Physiology and Biophysics, University of Iowa College of Medicine, Iowa City 52242.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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