Abstract
Smooth endoplasmic reticulum vesicles from rat liver display an ATP-supported Ca 2+ transport which is mediated by a (Ca 2+ + Mg 2+)-ATPase. During the catalytic cycle the terminal phosphate from ATP is incorporated to form an acid-precipitable reaction product(118 000-M r in SDS-gel electrophoresis) with stability characteristics of an acylphosphate. Comparative studies with sarcoplasmic reticulum vesicles from fast-twitch skeletal muscle suggest that the 118 000-M r phosphopeptide may be identified with the phosphorylated reaction intermediate of a Ca 2+ transport ATPase in endoplasmic reticulum, similar to that in sarcoplasmic reticulum of muscle.
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