Abstract
Abstract Human erythrocyte membrane protein components have been phosphorylated by an endogenous protein kinase. This transfer of phosphate from [γ-32P]ATP was stimulated by cyclic adenosine 3',5'-monophosphate and inhibited by calcium. The formation of phosphoserine and phosphothreonine bonds and the negligible effect of large changes in sodium and potassium concentrations clearly differentiate this phosphorylation from Na,K-ATPase activity.
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