dc.creatorDonoso Laurent, Paulina
dc.creatorBeltrán, Marianela
dc.creatorHidalgo Tapia, María Cecilia
dc.date.accessioned2019-01-29T16:00:04Z
dc.date.available2019-01-29T16:00:04Z
dc.date.created2019-01-29T16:00:04Z
dc.date.issued1996
dc.identifierBiochemistry, Volumen 35, Issue 41, 2018, Pages 13419-13425
dc.identifier00062960
dc.identifier10.1021/bi9616209
dc.identifierhttps://repositorio.uchile.cl/handle/2250/163027
dc.description.abstractCalcium binding to triads isolated from rabbit skeletal muscle followed a single hyperbolic function in the pH range 5.5-8.0. Maximal binding was obtained at pH 8.0; decreasing the pH decreased the binding capacity and, at pH ≤6.0, increased K(d) 2-fold. These results indicate that lowering the pH diminished calcium binding to calsequestrin, since this protein is the primary source of calcium binding sites in triads. Luminal pH had a marked effect on calcium release induced by 2 mM ATP, at pCa 5.0, pH 6.8. At a constant lutninal [Ca2+] of 0.1 mM, release rate constants (k) and initial rates of release increased steadily as a function of decreasing luminal pH; at luminal pH 7.5, values of k < 0.4 s-1 were found, whereas at pH 5.5 values of k ≃ 10 s-1 were obtained. Increasing luminal [Ca2+] from 0.05 mM to 0.7 mM had no effect on the k values measured at luminal pH 5.5. In contrast, at pH 6.8, increasing luminal [Ca2+] produced a marked increase in k values, that reached maximal values
dc.languageen
dc.rightshttp://creativecommons.org/licenses/by-nc-nd/3.0/cl/
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 Chile
dc.sourceBiochemistry
dc.subjectBiochemistry
dc.titleLuminal pH regulates calcium release kinetics in sarcoplasmic reticulum vesicles
dc.typeArtículo de revista


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