{"@context":{"@vocab":"https://cir.nii.ac.jp/schema/1.0/","rdfs":"http://www.w3.org/2000/01/rdf-schema#","dc":"http://purl.org/dc/elements/1.1/","dcterms":"http://purl.org/dc/terms/","foaf":"http://xmlns.com/foaf/0.1/","prism":"http://prismstandard.org/namespaces/basic/2.0/","cinii":"http://ci.nii.ac.jp/ns/1.0/","datacite":"https://schema.datacite.org/meta/kernel-4/","ndl":"http://ndl.go.jp/dcndl/terms/","jpcoar":"https://github.com/JPCOAR/schema/blob/master/2.0/"},"@id":"https://cir.nii.ac.jp/crid/1360574095612490752.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1093/oxfordjournals.jbchem.a121913"}},{"identifier":{"@type":"URI","@value":"http://academic.oup.com/jb/article-pdf/101/2/291/2311242/101-2-291.pdf"}},{"identifier":{"@type":"PMID","@value":"2953710"}}],"dc:title":[{"@value":"Ca2+- and Sr2+-Sensitivity of the ATPase Activity of Rabbit Skeletal Myofibrils: Effect of the Complete Substitution of Troponin C with Cardiac Troponin C, Calmodulin, and Parvalbumins1"}],"description":[{"notation":[{"@value":"The Ca2+-sensitive ATPase activity of rabbit skeletal myofibrils disappeared completely after treatment with a solution containing CDTA, a strong divalent cation chelator, at a low ionic strength. A gel electrophoretic study revealed that all troponin C and about half of myosin light chain 2 were removed from the myofibrils by the CDTA treatment. The CDTA-treated myofibrils, when reconstituted with skeletal troponin C, showed almost exactly the same Ca2+- or Sr2+-sensitive ATPase activity as that of intact myofibrils. The CDTA-treated myofibrils reconstituted with porcine cardiac troponin C showed the same Ca2+- or Sr2+-sensitivity of the ATPase as that of porcine cardiac myofibrils; Sr2+-sensitivity relative to Ca2+-sensitivity was about ten times higher than, and the maximal slope of the activation curve was about half that of skeletal myofibrils. These findings indicate that these characteristic features of divalent cation regulation in the contraction of skeletal and cardiac muscles are determined solely by the species of troponin C. Bovine brain calmodulin hardly activated the ATPase activity of the CDTA-treated myofibrils even in the presence of Ca2+. Excess calmodulin, however, was found to give Ca2+- or Sr2+-sensitivity to the ATPase activity of the CDTA-treated myofibrils. Frog skeletal parvalbumins 1 and 2, even in excess, did not affect the ATPase activity of the CDTA-treated myofibrils."}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1380574095612490752","@type":"Researcher","foaf:name":[{"@value":"Sachio MORIMOTO"}]},{"@id":"https://cir.nii.ac.jp/crid/1380574095612490753","@type":"Researcher","foaf:name":[{"@value":"Iwao OHTSUKI"}]}],"publication":{"publicationIdentifier":[{"@type":"EISSN","@value":"17562651"},{"@type":"PISSN","@value":"0021924X"},{"@type":"PISSN","@value":"http://id.crossref.org/issn/0021924X"}],"prism:publicationName":[{"@value":"The Journal of Biochemistry"}],"dc:publisher":[{"@value":"Oxford University Press (OUP)"}],"prism:publicationDate":"1987-02","prism:volume":"101","prism:number":"2","prism:startingPage":"291","prism:endingPage":"301"},"reviewed":"false","url":[{"@id":"http://academic.oup.com/jb/article-pdf/101/2/291/2311242/101-2-291.pdf"}],"createdAt":"2017-02-03","modifiedAt":"2017-08-23","foaf:topic":[{"@id":"https://cir.nii.ac.jp/all?q=Adenosine%20Triphosphatases","dc:title":"Adenosine Triphosphatases"},{"@id":"https://cir.nii.ac.jp/all?q=Myocardium","dc:title":"Myocardium"},{"@id":"https://cir.nii.ac.jp/all?q=Troponin","dc:title":"Troponin"},{"@id":"https://cir.nii.ac.jp/all?q=Enzyme%20Activation","dc:title":"Enzyme Activation"},{"@id":"https://cir.nii.ac.jp/all?q=Parvalbumins","dc:title":"Parvalbumins"},{"@id":"https://cir.nii.ac.jp/all?q=Calmodulin","dc:title":"Calmodulin"},{"@id":"https://cir.nii.ac.jp/all?q=Myofibrils","dc:title":"Myofibrils"},{"@id":"https://cir.nii.ac.jp/all?q=Strontium","dc:title":"Strontium"},{"@id":"https://cir.nii.ac.jp/all?q=Animals","dc:title":"Animals"},{"@id":"https://cir.nii.ac.jp/all?q=Calcium","dc:title":"Calcium"},{"@id":"https://cir.nii.ac.jp/all?q=Rabbits","dc:title":"Rabbits"},{"@id":"https://cir.nii.ac.jp/all?q=Troponin%20C","dc:title":"Troponin C"},{"@id":"https://cir.nii.ac.jp/all?q=Edetic%20Acid","dc:title":"Edetic Acid"}],"relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1390282679249293568","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Towards Understanding Mechanisms of Drug Action and Functions of the Body on the Molecular Level. Molecular mechanisms of calcium regulation of striated muscle contraction and its genetic disorder."},{"@language":"ja","@value":"薬の作用機序と生体機能の分子的理解に向けて　　筋収縮カルシウム受容調節の分子機構と遺伝性機能障害"},{"@value":"筋収縮カルシウム受容調節の分子機構と遺伝性機能障害"},{"@language":"ja-Kana","@value":"キンシュウシュク カルシウム ジュヨウ チョウセツ ノ ブンシ キコウ ト イデンセイ キノウ ショウガイ"}]},{"@id":"https://cir.nii.ac.jp/crid/1390282680153208704","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"SCH00013, a Novel Ca2+ Sensitizer With Positive Inotropic and No Chronotropic Action in Heart Failure"},{"@value":"SCH00013, a Novel Ca〔2+〕 Sensitizer With Positive Inotropic and No Chronotropic Action in Heart Failure"}]}],"dataSourceIdentifier":[{"@type":"CROSSREF","@value":"10.1093/oxfordjournals.jbchem.a121913"},{"@type":"OPENAIRE","@value":"doi_dedup___::d1ebdee31f54c0441d002f2d22987f2a"},{"@type":"CROSSREF","@value":"10.1254/jphs.fp0040654_references_DOI_Pdq7mAUYRSNACHqdSguVbsKtX8c"},{"@type":"CROSSREF","@value":"10.1254/fpj.118.147_references_DOI_Pdq7mAUYRSNACHqdSguVbsKtX8c"}]}