Solubilized monomeric sarcoplasmic reticulum Ca pump protein

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Abstract
Phosphorylation (by inorganic phosphate) of sarcoplasmic reticulum Ca pump protein has been studied in a detergent solution in which the protein has been previously shown to exist as a monomer. The course of the reaction is qualitatively similar to that observed for membrane‐bound (possibly oligomeric) protein. In particular, the results indicate that alternation between the two principal conformational states of the Ca pump protein persists in the monomeric state, which suggests that the machinery for coupling of ATP hydrolysis to Ca2+ transport is intact. There are quantitative differences between monomeric and membrane‐bound protein with respect to phosphorylation, but they are not necessarily related to the state of association.