| pubmed-article:6250577 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6250577 | lifeskim:mentions | umls-concept:C0006772 | lld:lifeskim |
| pubmed-article:6250577 | lifeskim:mentions | umls-concept:C0332157 | lld:lifeskim |
| pubmed-article:6250577 | lifeskim:mentions | umls-concept:C0205148 | lld:lifeskim |
| pubmed-article:6250577 | lifeskim:mentions | umls-concept:C0598629 | lld:lifeskim |
| pubmed-article:6250577 | pubmed:issue | 16 | lld:pubmed |
| pubmed-article:6250577 | pubmed:dateCreated | 1980-11-24 | lld:pubmed |
| pubmed-article:6250577 | pubmed:abstractText | Interactions between calmodulin (CaM) and several hydrophobic fluorescent probes were characterized in order to determine if CaM expresses hydrophobic binding sites in the presence of Ca2+. Several classes of fluorescent probes capable of sensing exposure of hydrophobic binding sites on proteins were found to bind to CaM, and these interactions were greatly enhanced by Ca2+. In the presence of Ca2+, the fluorescence intensity of 9-anthroylcholine (9AC) was increased 24-fold by CaM, with a shift in the fluorescence emission maximum from 514 to 486 nm. The fluorescence intensity of 8-anilino-1-naphthalenesulfonate (Ans) was enhanced 27-fold with an emission maximum shift from 540 to 488 nm in the presence of CaM and Ca2+. Similar results were obtained with the uncharged fluorescent ligand, N-phyenyl-1-naphthylamine. With all three fluorescent dyes, the fluorescence changes caused by CaM in the absence of Ca2+ were minor compared to those observed with CaM and Ca2+. Direct binding studies using equilibrium dialysis demonstrated that CaM can bind four to six molecules of 9AC or two to three molecules of Ans in a calcium-dependent manner. The effects of various amphiphilic compounds on the Ca2+-dependent complex formation between CaM and the Ca2+-sensitive phosphodiesterase or troponin I were investigated. Trifluoperazine (TFP) and 9AC inhibited CaM stimulation of the Ca2+-sensitive phosphodiesterase. The Ca2+-dependent binding of the phosphodiesterase to CaM-Sepharose was also inhibited by TFP, 9AC, and Ans. Furthermore, binding of CaM to troponin I-Sepharose was inhibited by these ligands. Consistent with these data was the observation that troponin I antagonized binding of 9AC to CaM. These data indicate that binding of Ca2+ to CaM results in exposure of a domain with considerable hydrophobic character, and binding of hydrophobic ligands to this domain antagonizes CaM-protein interactions. It is proposed that this hydrophobic domain may serve as the interface for the Ca2+-dependent binding of CaM to the phosphodiesterase or troponin I. | lld:pubmed |
| pubmed-article:6250577 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6250577 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6250577 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:6250577 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6250577 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:6250577 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:6250577 | pubmed:author | pubmed-author:StoryD FDF | lld:pubmed |
| pubmed-article:6250577 | pubmed:author | pubmed-author:LaPorteD CDC | lld:pubmed |
| pubmed-article:6250577 | pubmed:author | pubmed-author:WiermanB MBM | lld:pubmed |
| pubmed-article:6250577 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6250577 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:6250577 | pubmed:volume | 19 | lld:pubmed |
| pubmed-article:6250577 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6250577 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6250577 | pubmed:pagination | 3814-9 | lld:pubmed |
| pubmed-article:6250577 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:6250577 | pubmed:year | 1980 | lld:pubmed |
| pubmed-article:6250577 | pubmed:articleTitle | Calcium-induced exposure of a hydrophobic surface on calmodulin. | lld:pubmed |
| pubmed-article:6250577 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6250577 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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