| pubmed-article:6841341 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6841341 | lifeskim:mentions | umls-concept:C0034493 | lld:lifeskim |
| pubmed-article:6841341 | lifeskim:mentions | umls-concept:C0242692 | lld:lifeskim |
| pubmed-article:6841341 | lifeskim:mentions | umls-concept:C0077401 | lld:lifeskim |
| pubmed-article:6841341 | lifeskim:mentions | umls-concept:C0077404 | lld:lifeskim |
| pubmed-article:6841341 | lifeskim:mentions | umls-concept:C0041197 | lld:lifeskim |
| pubmed-article:6841341 | lifeskim:mentions | umls-concept:C0077400 | lld:lifeskim |
| pubmed-article:6841341 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:6841341 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:6841341 | pubmed:dateCreated | 1983-6-17 | lld:pubmed |
| pubmed-article:6841341 | pubmed:abstractText | The binding of the chymotryptic troponin T subfragments to tropomyosin, troponin I, and troponin C was semiquantitatively examined by using affinity chromatography, and also by co-sedimentation with F-actin and polyacrylamide gel electrophoresis in 14 mM Tris/90 mM glycine. Circular dichroism spectra of the subfragments were measured to confirm that the subfragments retained their conformational structures. Based on these results, the binding sites of tropomyosin, troponin I, and troponin C on the troponin T sequence were elucidated. Tropomyosin bound mainly to the region of troponin T1 (residues 1-158) with the same binding strength as to the original troponin T. The C-terminal region of troponin T (residues 243-259) was the second binding site to tropomyosin under physiological conditions. The binding site of troponin I was concluded to be the region including residues 223-227. The binding of troponin C was dependent on Ca2+ ion concentration. The C-terminal region of troponin T2 (residues 159-259) was indicated to be the Ca2+-independent troponin C-binding site and the N-terminal side of troponin T2 to be the Ca2+-dependent site. | lld:pubmed |
| pubmed-article:6841341 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6841341 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6841341 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:6841341 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6841341 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6841341 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6841341 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6841341 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6841341 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6841341 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6841341 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6841341 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6841341 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:6841341 | pubmed:issn | 0021-924X | lld:pubmed |
| pubmed-article:6841341 | pubmed:author | pubmed-author:TanokuraMM | lld:pubmed |
| pubmed-article:6841341 | pubmed:author | pubmed-author:OnoAA | lld:pubmed |
| pubmed-article:6841341 | pubmed:author | pubmed-author:TawadaYY | lld:pubmed |
| pubmed-article:6841341 | pubmed:author | pubmed-author:OhtsukiII | lld:pubmed |
| pubmed-article:6841341 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6841341 | pubmed:volume | 93 | lld:pubmed |
| pubmed-article:6841341 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6841341 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6841341 | pubmed:pagination | 331-7 | lld:pubmed |
| pubmed-article:6841341 | pubmed:dateRevised | 2007-12-19 | lld:pubmed |
| pubmed-article:6841341 | pubmed:meshHeading | pubmed-meshheading:6841341-... | lld:pubmed |
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| pubmed-article:6841341 | pubmed:meshHeading | pubmed-meshheading:6841341-... | lld:pubmed |
| pubmed-article:6841341 | pubmed:meshHeading | pubmed-meshheading:6841341-... | lld:pubmed |
| pubmed-article:6841341 | pubmed:meshHeading | pubmed-meshheading:6841341-... | lld:pubmed |
| pubmed-article:6841341 | pubmed:meshHeading | pubmed-meshheading:6841341-... | lld:pubmed |
| pubmed-article:6841341 | pubmed:meshHeading | pubmed-meshheading:6841341-... | lld:pubmed |
| pubmed-article:6841341 | pubmed:meshHeading | pubmed-meshheading:6841341-... | lld:pubmed |
| pubmed-article:6841341 | pubmed:meshHeading | pubmed-meshheading:6841341-... | lld:pubmed |
| pubmed-article:6841341 | pubmed:meshHeading | pubmed-meshheading:6841341-... | lld:pubmed |
| pubmed-article:6841341 | pubmed:year | 1983 | lld:pubmed |
| pubmed-article:6841341 | pubmed:articleTitle | Chymotryptic subfragments of troponin T from rabbit skeletal muscle. Interaction with tropomyosin, troponin I and troponin C. | lld:pubmed |
| pubmed-article:6841341 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6841341 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:6841341 | lld:pubmed |
