pubmed-article:2925646 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2925646 | lifeskim:mentions | umls-concept:C0032098 | lld:lifeskim |
pubmed-article:2925646 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
pubmed-article:2925646 | lifeskim:mentions | umls-concept:C0006787 | lld:lifeskim |
pubmed-article:2925646 | lifeskim:mentions | umls-concept:C2700400 | lld:lifeskim |
pubmed-article:2925646 | pubmed:issue | 8 | lld:pubmed |
pubmed-article:2925646 | pubmed:dateCreated | 1989-4-25 | lld:pubmed |
pubmed-article:2925646 | 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. | lld:pubmed |
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pubmed-article:2925646 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2925646 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2925646 | pubmed:language | eng | lld:pubmed |
pubmed-article:2925646 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2925646 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:2925646 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2925646 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2925646 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2925646 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2925646 | pubmed:month | Mar | lld:pubmed |
pubmed-article:2925646 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:2925646 | pubmed:author | pubmed-author:KrauseK HKH | lld:pubmed |
pubmed-article:2925646 | pubmed:author | pubmed-author:CampbellK PKP | lld:pubmed |
pubmed-article:2925646 | pubmed:author | pubmed-author:ThomasM AMA | lld:pubmed |
pubmed-article:2925646 | pubmed:author | pubmed-author:ChowKK | lld:pubmed |
pubmed-article:2925646 | pubmed:author | pubmed-author:SjolundR DRD | lld:pubmed |
pubmed-article:2925646 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2925646 | pubmed:day | 15 | lld:pubmed |
pubmed-article:2925646 | pubmed:volume | 264 | lld:pubmed |
pubmed-article:2925646 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2925646 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2925646 | pubmed:pagination | 4269-72 | lld:pubmed |
pubmed-article:2925646 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:2925646 | pubmed:year | 1989 | lld:pubmed |
pubmed-article:2925646 | pubmed:articleTitle | Plant cells contain calsequestrin. | lld:pubmed |
pubmed-article:2925646 | pubmed:affiliation | Department of Physiology and Biophysics, University of Iowa College of Medicine, Iowa City 52242. | lld:pubmed |
pubmed-article:2925646 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2925646 | pubmed:publicationType | Comparative Study | lld:pubmed |
pubmed-article:2925646 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:2925646 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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