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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1983-6-10
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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.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/6847627-1180911,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6847627-131972,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6847627-137127,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6847627-171969,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6847627-179535,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6847627-181375,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6847627-4262960,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6847627-435249,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6847627-4369265,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6847627-4369337,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6847627-4377105,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6847627-4713300,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6847627-4824205,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6847627-4852584,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6847627-4855003,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6847627-520312,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6847627-5440908,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6847627-5550981,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6847627-5673536,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6847627-6450206,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6847627-6460759,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6847627-6804229,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6847627-7103951,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6847627-7236209,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6847627-7242669,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6847627-811252
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium Chloride,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Calmodulin,
http://linkedlifedata.com/resource/pubmed/chemical/Imidoesters,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Muscle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Troponin,
http://linkedlifedata.com/resource/pubmed/chemical/Troponin C,
http://linkedlifedata.com/resource/pubmed/chemical/Troponin I
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
209
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
417-26
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:6847627-Amino Acids,
pubmed-meshheading:6847627-Animals,
pubmed-meshheading:6847627-Calcium Chloride,
pubmed-meshheading:6847627-Calcium-Binding Proteins,
pubmed-meshheading:6847627-Calmodulin,
pubmed-meshheading:6847627-Chromatography, Gel,
pubmed-meshheading:6847627-Imidoesters,
pubmed-meshheading:6847627-Macromolecular Substances,
pubmed-meshheading:6847627-Molecular Weight,
pubmed-meshheading:6847627-Muscle Proteins,
pubmed-meshheading:6847627-Peptide Fragments,
pubmed-meshheading:6847627-Rabbits,
pubmed-meshheading:6847627-Troponin,
pubmed-meshheading:6847627-Troponin C,
pubmed-meshheading:6847627-Troponin I
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pubmed:year |
1983
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pubmed:articleTitle |
Studies of the interaction of troponin I with proteins of the I-filament and calmodulin.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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