| pubmed-article:8253742 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8253742 | lifeskim:mentions | umls-concept:C0014792 | lld:lifeskim |
| pubmed-article:8253742 | lifeskim:mentions | umls-concept:C0229304 | lld:lifeskim |
| pubmed-article:8253742 | lifeskim:mentions | umls-concept:C0006772 | lld:lifeskim |
| pubmed-article:8253742 | lifeskim:mentions | umls-concept:C0001473 | lld:lifeskim |
| pubmed-article:8253742 | lifeskim:mentions | umls-concept:C0077400 | lld:lifeskim |
| pubmed-article:8253742 | lifeskim:mentions | umls-concept:C1707455 | lld:lifeskim |
| pubmed-article:8253742 | lifeskim:mentions | umls-concept:C1709915 | lld:lifeskim |
| pubmed-article:8253742 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:8253742 | pubmed:issue | 35 | lld:pubmed |
| pubmed-article:8253742 | pubmed:dateCreated | 1994-1-13 | lld:pubmed |
| pubmed-article:8253742 | pubmed:abstractText | Troponin C can replace calmodulin in the activation of the Ca(2+)-ATPase of pig erythrocytes provided that the reaction medium contains relatively high free Ca2+ concentrations (> 0.5 microM). In the presence of 10 microM free Ca2+, the troponin C-activated ATPase reaches a maximal velocity of approximately 70% of that attained with calmodulin. The half-maximal concentration for troponin C activation is about 200 times greater than for calmodulin. Troponin C displaces the half-maximal concentration for activation by Ca2+ to pCa 5.46 and the cooperativity between the Ca2+ binding sites to nH 1.1, compared with pCa 6.14 and nH 1.72 when calmodulin is used. Both EF-hand proteins also elicit activation by ATP at a nucleotide regulatory site, as well as a Ca(2+)-dependent p-nitrophenyl phosphatase activity. Troponin I prevents activation of the enzyme by troponin C. A mutant of troponin C with the amino-terminal helix deleted (NHdel) activates the Ca(2+)-ATPase to the same extent and with the same Ca2+ dependence as wild-type troponin C (rTnC); the half-maximal concentration for activation by NHdel is 2.5 times smaller than that for rTnC. We conclude that the structural features that distinguish the two EF-hand proteins affect their binding to the target enzyme more than their ability to transform the enzyme's response to Ca2+ or ATP. The differences in the amino-terminal domains of troponin C and calmodulin cannot account for the differences in ability of these proteins to activate the target system used as a model. | lld:pubmed |
| pubmed-article:8253742 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8253742 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8253742 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8253742 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8253742 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8253742 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8253742 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8253742 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8253742 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8253742 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8253742 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:8253742 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:8253742 | pubmed:author | pubmed-author:SmillieL BLB | lld:pubmed |
| pubmed-article:8253742 | pubmed:author | pubmed-author:SorensonM MMM | lld:pubmed |
| pubmed-article:8253742 | pubmed:author | pubmed-author:ScofanoH MHM | lld:pubmed |
| pubmed-article:8253742 | pubmed:author | pubmed-author:da SilvaE FEF | lld:pubmed |
| pubmed-article:8253742 | pubmed:author | pubmed-author:BarrabinHH | lld:pubmed |
| pubmed-article:8253742 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8253742 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:8253742 | pubmed:volume | 268 | lld:pubmed |
| pubmed-article:8253742 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8253742 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8253742 | pubmed:pagination | 26220-5 | lld:pubmed |
| pubmed-article:8253742 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
| pubmed-article:8253742 | pubmed:meshHeading | pubmed-meshheading:8253742-... | lld:pubmed |
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| pubmed-article:8253742 | pubmed:meshHeading | pubmed-meshheading:8253742-... | lld:pubmed |
| pubmed-article:8253742 | pubmed:meshHeading | pubmed-meshheading:8253742-... | lld:pubmed |
| pubmed-article:8253742 | pubmed:meshHeading | pubmed-meshheading:8253742-... | lld:pubmed |
| pubmed-article:8253742 | pubmed:meshHeading | pubmed-meshheading:8253742-... | lld:pubmed |
| pubmed-article:8253742 | pubmed:meshHeading | pubmed-meshheading:8253742-... | lld:pubmed |
| pubmed-article:8253742 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8253742 | pubmed:articleTitle | Comparison of calmodulin and troponin C with and without its amino-terminal helix (residues 1-11) in the activation of erythrocyte Ca(2+)-ATPase. | lld:pubmed |
| pubmed-article:8253742 | pubmed:affiliation | Departamento de Bioquímica Médica, Universidade Federal do Rio de Janeiro, Brazil. | lld:pubmed |
| pubmed-article:8253742 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8253742 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:8253742 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8253742 | lld:pubmed |
