| pubmed-article:1699445 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1699445 | lifeskim:mentions | umls-concept:C0035975 | lld:lifeskim |
| pubmed-article:1699445 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:1699445 | lifeskim:mentions | umls-concept:C1413043 | lld:lifeskim |
| pubmed-article:1699445 | lifeskim:mentions | umls-concept:C0242210 | lld:lifeskim |
| pubmed-article:1699445 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:1699445 | pubmed:dateCreated | 1990-11-7 | lld:pubmed |
| pubmed-article:1699445 | pubmed:abstractText | The interaction of ruthenium red, [(NH3)5Ru-O-Ru(NH3)4-O-Ru(NH3)5]Cl6.4H2O, with various Ca2(+)-binding proteins was studied. Ruthenium red inhibited Ca2+ binding to the sarcoplasmic reticulum protein, calsequestrin, immobilized on Sepharose 4B. Furthermore, ruthenium red bound to calsequestrin with high affinity (Kd = 0.7 microM; Bmax = 218 nmol/mg protein). The dye stained calsequestrin in sodium dodecyl sulfate-polyacrylamide gels or on nitrocellulose paper and was displaced by Ca2+ (Ki = 1.4 mM). The specificity of ruthenium red staining of several Ca2(+)-binding proteins was investigated by comparison with two other detection methods, 45Ca2+ autoradiography and the Stains-all reaction. Ruthenium red bound to the same proteins detected by the 45Ca2+ overlay technique. Ruthenium red stained both the erythrocyte Band 3 anion transporter and the Ca2(+)-ATPase of skeletal muscle sarcoplasmic reticulum. Ruthenium red also stained the EF hand conformation Ca2(+)-binding proteins, calmodulin, troponin C, and S-100. This inorganic dye provides a simple, rapid method for detecting various types of Ca2(+)-binding proteins following electrophoresis. | lld:pubmed |
| pubmed-article:1699445 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1699445 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1699445 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1699445 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1699445 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1699445 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1699445 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1699445 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:1699445 | pubmed:issn | 0003-2697 | lld:pubmed |
| pubmed-article:1699445 | pubmed:author | pubmed-author:ReithmeierR... | lld:pubmed |
| pubmed-article:1699445 | pubmed:author | pubmed-author:CharukJ HJH | lld:pubmed |
| pubmed-article:1699445 | pubmed:author | pubmed-author:PirragliaC... | lld:pubmed |
| pubmed-article:1699445 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1699445 | pubmed:volume | 188 | lld:pubmed |
| pubmed-article:1699445 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1699445 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1699445 | pubmed:pagination | 123-31 | lld:pubmed |
| pubmed-article:1699445 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:1699445 | pubmed:meshHeading | pubmed-meshheading:1699445-... | lld:pubmed |
| pubmed-article:1699445 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:1699445 | pubmed:articleTitle | Interaction of ruthenium red with Ca2(+)-binding proteins. | lld:pubmed |
| pubmed-article:1699445 | pubmed:affiliation | MRC Group in Membrane Biology, Department of Medicine, University of Toronto, Ontario, Canada. | lld:pubmed |
| pubmed-article:1699445 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1699445 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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