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Protons induce calsequestrin conformational changes
(Biophysical Society, 1996)
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 ...
Luminal pH regulates calcium release kinetics in sarcoplasmic reticulum vesicles
Calcium 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, ...
Luminal calcium regulates calcium release in triads isolated from frog and rabbit skeletal muscle
Triads isolated from frog and rabbit skeletal muscle were equilibrated with different external [Ca2+], ranging from 0.025 to 10 mM. Vesicular calcium increased with external [Ca2+] as the sum of a linear plus a saturable ...