Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/38358
DC FieldValueLanguage
dc.contributor.authorLiou, Y.M.en_US
dc.contributor.author劉英明zh_TW
dc.date2001zh_TW
dc.date.accessioned2014-06-06T08:00:44Z-
dc.date.available2014-06-06T08:00:44Z-
dc.identifier.issn0021-521Xzh_TW
dc.identifier.urihttp://hdl.handle.net/11455/38358-
dc.description.abstractLength dependence of cardiac Ca2+ activation is an essential component of the Frank-Starling relation. The aim of this study is to examine the length effects on the Ca2+-induced conformational changes of filament-bound cTnC in skinned cardiac muscle fibers. The two cysteine residues (Cys-35 and Cys-84) in the regulatory domain of cTnC allow for the attachment of conformational probes to this region. Their incorporation with the fluorescent probe, 7-diethylamino-3-[4 ' -maleimidylphenyl]-4-methylcoumarin (CPM), was used to determine the varying cTnC conformations in cardiac fibers. The data obtained show that the length-dependent Ca2+-mediated conformational changes require strong-binding cross-bridges for cardiac activation.en_US
dc.language.isoen_USzh_TW
dc.relationJapanese Journal of Physiologyen_US
dc.relation.ispartofseriesJapanese Journal of Physiology, Volume 51, Issue 3, Page(s) 385-388.en_US
dc.relation.urihttp://dx.doi.org/10.2170/jjphysiol.51.385en_US
dc.subjectFrank-Starling relationen_US
dc.subjectfilament-bound cTnCen_US
dc.subjectCPM incorporationen_US
dc.subjectcalcium-bindingen_US
dc.subjectskeletal-muscleen_US
dc.subjectactinen_US
dc.subjectrigoren_US
dc.subjectfluorescenceen_US
dc.subjectmyofibrilsen_US
dc.subjecttensionen_US
dc.subjectcys-84en_US
dc.titleEffects of sarcomere length and Ca2+ binding on SH reactivity of myofilament bound troponin C in porcine skinned cardiac muscle fibersen_US
dc.typeJournal Articlezh_TW
dc.identifier.doi10.2170/jjphysiol.51.385zh_TW
Appears in Collections:生命科學系所
文件中的檔案:

取得全文請前往華藝線上圖書館



Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.