Rate of calcium release and ATP synthesis in sarcoplasmic reticulum vesicles

Abstract

Sarcoplasmic reticulum vesicles can catalyze the synthesis of ATP coupled to the efflux of calcium. The rate of this reaction is much faster when the vesicles are loaded in a medium containing phosphate than when oxalate is the precipitating agent. Two components of ATP synthesis can be observed when vesicles loaded with calcium phosphate are used. In the millisecond range and when the loaded vesicles are phosphorylated by Pi, the addition of ADP leads to an initial burst of ATP synthesis and after 50 ms approximately 3.0 nmol of ATP/mg protein are synthesized. This burst is not inhibited by ATP and is enhanced by physiological concentrations of KCl. The slow component of ATP synthesis is inhibited by both ATP and 100 mM KCl. In the physiological pH range, betaine, a trimethylamine present in different tissues, increases the level of phosphoenzyme formed by Pi and enhances the amount of ATP synthesized during the first turn of the reversal of the calcium pump.