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| pubmed-article:6450619 | lifeskim:mentions | umls-concept:C0036226 | lld:lifeskim |
| pubmed-article:6450619 | lifeskim:mentions | umls-concept:C0001473 | lld:lifeskim |
| pubmed-article:6450619 | lifeskim:mentions | umls-concept:C0392360 | lld:lifeskim |
| pubmed-article:6450619 | lifeskim:mentions | umls-concept:C0060520 | lld:lifeskim |
| pubmed-article:6450619 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:6450619 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:6450619 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:6450619 | lifeskim:mentions | umls-concept:C0443172 | lld:lifeskim |
| pubmed-article:6450619 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:6450619 | pubmed:dateCreated | 1981-4-13 | lld:pubmed |
| pubmed-article:6450619 | pubmed:abstractText | Fluorescein isothiocyanate is a highly specific inhibitor of the Ca2+-ATPase from sarcoplasmic reticulum. The Ca2+ pumping is inhibited completely at a fluorescein isothiocyanate concentration half that of the ATPase protein, indicating that the protein is at least a dimer. ATP protected specifically against fluorescein isothiocyanate inhibition, indicating that fluorescein isothiocyanate may react at the nucleotide binding site of the ATPase (probably with a reactive lysine residue). The fluorescein is incorporated almost exclusively into the 105 kdalton catalytic polypeptide of the ATPase and digestion by trypsin gives rise to a fluorescein-labelled 45 kdalton fragment. Conformational changes induced by addition of Ca can be studied conveniently with the fluorescein-labelled ATPase. | lld:pubmed |
| pubmed-article:6450619 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6450619 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6450619 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:6450619 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6450619 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:6450619 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:6450619 | pubmed:author | pubmed-author:PickUU | lld:pubmed |
| pubmed-article:6450619 | pubmed:author | pubmed-author:KarlishS JSJ | lld:pubmed |
| pubmed-article:6450619 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6450619 | pubmed:day | 20 | lld:pubmed |
| pubmed-article:6450619 | pubmed:volume | 626 | lld:pubmed |
| pubmed-article:6450619 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6450619 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6450619 | pubmed:pagination | 255-61 | lld:pubmed |
| pubmed-article:6450619 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:6450619 | pubmed:year | 1980 | lld:pubmed |
| pubmed-article:6450619 | pubmed:articleTitle | Indications for an oligomeric structure and for conformational changes in sarcoplasmic reticulum Ca2+-ATPase labelled selectively with fluorescein. | lld:pubmed |
| pubmed-article:6450619 | pubmed:publicationType | Journal Article | lld:pubmed |
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