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Authordc.contributor.authorHidalgo Tapia, María Cecilia 
Authordc.contributor.authorDonoso Laurent, Paulina 
Authordc.contributor.authorRodriguez, Patricio H. 
Cita de ítemdc.identifier.citationBiophysical Journal, Volumen 71, Issue 4, 2018, Pages 2130-2137
Abstractdc.description.abstractCalsequestrin, a high-capacity, intermediate-affinity, calcium-binding protein present in the lumen of sarcoplasmic reticulum, undergoes extensive calcium-induced conformational changes at neutral pH that cause distinct intrinsic fluorescence changes. The results reported in this work indicate that pH has a marked effect on these calcium-induced intrinsic fluorescence changes, as well as on calorimetric changes produced by the addition of Ca2+ to calsequestrin. The addition of Ca2+ at neutral pH produced a marked and cooperative increase in calsequestrin intrinsic fluorescence. In contrast, at pH 6.0 calsequestrin's intrinsic fluorescence was not affected by the addition of Ca2+, and the same intrinsic fluorescence as that measured in millimolar calcium at neutral pH was obtained. The magnitude and the cooperativity of the calcium-induced intrinsic fluorescence changes decreased as either [H+] or [K+] increased. The evolution of heat production, determined by microcalorimetry, observed
Publisherdc.publisherBiophysical Society
Type of licensedc.rightsAttribution-NonCommercial-NoDerivs 3.0 Chile
Link to Licensedc.rights.uri
Sourcedc.sourceBiophysical Journal
Títulodc.titleProtons induce calsequestrin conformational changes
Document typedc.typeArtículo de revista
Indexationuchile.indexArtículo de publicación SCOPUS

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Attribution-NonCommercial-NoDerivs 3.0 Chile
Except where otherwise noted, this item's license is described as Attribution-NonCommercial-NoDerivs 3.0 Chile