| pubmed-article:6847627 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6847627 | lifeskim:mentions | umls-concept:C0006772 | lld:lifeskim |
| pubmed-article:6847627 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:6847627 | lifeskim:mentions | umls-concept:C0077401 | lld:lifeskim |
| pubmed-article:6847627 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:6847627 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:6847627 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:6847627 | pubmed:dateCreated | 1983-6-10 | lld:pubmed |
| pubmed-article:6847627 | pubmed:abstractText | 1. All lysine residues in native troponin I from rabbit fast-twitch skeletal muscle reacted with methyl acetimidate and ethyl acetimidate. 2. The reactivity of lysine-18 of troponin I to acetimidate was much diminished when the troponin I was complexed in the presence of Ca2+ with troponin C alone or in the whole troponin complex. 3. In the presence of EGTA, lysine-18 of troponin I in the troponin I-troponin C complex was more reactive to acetimidate than it was in the presence of Ca2+. 4. No masking of lysine residues could be detected when troponin I interacted with calmodulin or actin. 5. Sedimentation-equilibrium studies indicated that the complex of troponin I with calmodulin was more readily dissociated in the absence of Ca2+ than was its complex with troponin C under otherwise identical conditions. 6. These studies suggest that the nature of the involvement of the N-terminal region of troponin I is a major difference between its modes of interaction with calmodulin and with troponin C. | lld:pubmed |
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| pubmed-article:6847627 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:6847627 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:6847627 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6847627 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:6847627 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:6847627 | pubmed:author | pubmed-author:GrandR JRJ | lld:pubmed |
| pubmed-article:6847627 | pubmed:author | pubmed-author:TrayerI PIP | lld:pubmed |
| pubmed-article:6847627 | pubmed:author | pubmed-author:PerryS VSV | lld:pubmed |
| pubmed-article:6847627 | pubmed:author | pubmed-author:MockB HBH | lld:pubmed |
| pubmed-article:6847627 | pubmed:author | pubmed-author:OrdidgeMM | lld:pubmed |
| pubmed-article:6847627 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6847627 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:6847627 | pubmed:volume | 209 | lld:pubmed |
| pubmed-article:6847627 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6847627 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6847627 | pubmed:pagination | 417-26 | lld:pubmed |
| pubmed-article:6847627 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:6847627 | pubmed:year | 1983 | lld:pubmed |
| pubmed-article:6847627 | pubmed:articleTitle | Studies of the interaction of troponin I with proteins of the I-filament and calmodulin. | lld:pubmed |
| pubmed-article:6847627 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6847627 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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