dc.creator | Hidalgo Tapia, María Cecilia | |
dc.creator | Donoso Laurent, Paulina | |
dc.creator | Rodriguez, Patricio H. | |
dc.date.accessioned | 2019-01-29T16:00:07Z | |
dc.date.available | 2019-01-29T16:00:07Z | |
dc.date.created | 2019-01-29T16:00:07Z | |
dc.date.issued | 1996 | |
dc.identifier | Biophysical Journal, Volumen 71, Issue 4, 2018, Pages 2130-2137 | |
dc.identifier | 00063495 | |
dc.identifier | 10.1016/S0006-3495(96)79413-4 | |
dc.identifier | https://repositorio.uchile.cl/handle/2250/163036 | |
dc.description.abstract | Calsequestrin, 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 | |
dc.language | en | |
dc.publisher | Biophysical Society | |
dc.rights | http://creativecommons.org/licenses/by-nc-nd/3.0/cl/ | |
dc.rights | Attribution-NonCommercial-NoDerivs 3.0 Chile | |
dc.source | Biophysical Journal | |
dc.subject | Biophysics | |
dc.title | Protons induce calsequestrin conformational changes | |
dc.type | Artículos de revistas | |