| pubmed-article:2932440 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2932440 | lifeskim:mentions | umls-concept:C0036226 | lld:lifeskim |
| pubmed-article:2932440 | lifeskim:mentions | umls-concept:C1330957 | lld:lifeskim |
| pubmed-article:2932440 | lifeskim:mentions | umls-concept:C0001473 | lld:lifeskim |
| pubmed-article:2932440 | lifeskim:mentions | umls-concept:C1704632 | lld:lifeskim |
| pubmed-article:2932440 | lifeskim:mentions | umls-concept:C0871261 | lld:lifeskim |
| pubmed-article:2932440 | lifeskim:mentions | umls-concept:C2911692 | lld:lifeskim |
| pubmed-article:2932440 | lifeskim:mentions | umls-concept:C1706817 | lld:lifeskim |
| pubmed-article:2932440 | lifeskim:mentions | umls-concept:C1514468 | lld:lifeskim |
| pubmed-article:2932440 | lifeskim:mentions | umls-concept:C0596311 | lld:lifeskim |
| pubmed-article:2932440 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:2932440 | pubmed:issue | 25 | lld:pubmed |
| pubmed-article:2932440 | pubmed:dateCreated | 1985-12-5 | lld:pubmed |
| pubmed-article:2932440 | pubmed:abstractText | Trypsin cleaves the Ca2+-ATPase of sarcoplasmic reticulum into two major fragments (A and B), followed by subsequent cleavage into smaller peptides. Although the ATP-dependent Ca2+ transport is still observed after cleavage of the ATPase into the A and B fragments, the Ca2+ transport energized by acetyl phosphate is strongly inhibited. Covalent labeling of the Ca2+-ATPase by fluorescein 5'-isothiocyanate inhibited both the ATP and acetyl phosphate-dependent Ca2+ transport. Vanadate protected the A and B fragments from further hydrolysis and preserved the ability of the cleaved Ca2+-ATPase to form crystals and to show the characteristic conformational changes in response to Ca2+ and EGTA that are observed with the intact enzyme. The protective effect of vanadate may be useful for the isolation of the A and B fragments in functional form. | lld:pubmed |
| pubmed-article:2932440 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2932440 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2932440 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2932440 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2932440 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2932440 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2932440 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2932440 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2932440 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2932440 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2932440 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2932440 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2932440 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2932440 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2932440 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:2932440 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:2932440 | pubmed:author | pubmed-author:PappSS | lld:pubmed |
| pubmed-article:2932440 | pubmed:author | pubmed-author:MartonosiAA | lld:pubmed |
| pubmed-article:2932440 | pubmed:author | pubmed-author:DuxLL | lld:pubmed |
| pubmed-article:2932440 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2932440 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:2932440 | pubmed:volume | 260 | lld:pubmed |
| pubmed-article:2932440 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2932440 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2932440 | pubmed:pagination | 13454-8 | lld:pubmed |
| pubmed-article:2932440 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
| pubmed-article:2932440 | pubmed:meshHeading | pubmed-meshheading:2932440-... | lld:pubmed |
| pubmed-article:2932440 | pubmed:meshHeading | pubmed-meshheading:2932440-... | lld:pubmed |
| pubmed-article:2932440 | pubmed:meshHeading | pubmed-meshheading:2932440-... | lld:pubmed |
| pubmed-article:2932440 | pubmed:meshHeading | pubmed-meshheading:2932440-... | lld:pubmed |
| pubmed-article:2932440 | pubmed:meshHeading | pubmed-meshheading:2932440-... | lld:pubmed |
| pubmed-article:2932440 | pubmed:meshHeading | pubmed-meshheading:2932440-... | lld:pubmed |
| pubmed-article:2932440 | pubmed:meshHeading | pubmed-meshheading:2932440-... | lld:pubmed |
| pubmed-article:2932440 | pubmed:meshHeading | pubmed-meshheading:2932440-... | lld:pubmed |
| pubmed-article:2932440 | pubmed:meshHeading | pubmed-meshheading:2932440-... | lld:pubmed |
| pubmed-article:2932440 | pubmed:meshHeading | pubmed-meshheading:2932440-... | lld:pubmed |
| pubmed-article:2932440 | pubmed:meshHeading | pubmed-meshheading:2932440-... | lld:pubmed |
| pubmed-article:2932440 | pubmed:meshHeading | pubmed-meshheading:2932440-... | lld:pubmed |
| pubmed-article:2932440 | pubmed:meshHeading | pubmed-meshheading:2932440-... | lld:pubmed |
| pubmed-article:2932440 | pubmed:meshHeading | pubmed-meshheading:2932440-... | lld:pubmed |
| pubmed-article:2932440 | pubmed:year | 1985 | lld:pubmed |
| pubmed-article:2932440 | pubmed:articleTitle | Conformational responses of the tryptic cleavage products of the Ca2+-ATPase of sarcoplasmic reticulum. | lld:pubmed |
| pubmed-article:2932440 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2932440 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:2932440 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2932440 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:2932440 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2932440 | lld:pubmed |
