PHOSPHORYLATION IN VITRO OF ADRENAL SUBCELLULAR PROTEINS BY ADENOSINE-3′, 5′-MONOPHOSPHATE-DEPENDENT PROTEIN KINASE: EFFECT OF ACTH IN VIVO

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Abstract
In vitro phosphorylation of protein from rat adrenal subcellular fractions by partially purified cAMP-dependent protein kinase isolated from rat adrenal and liver was investigated. Only proteins from microsomes were found to be a good substrate for the enzyme. Rates of phosphorylation of adrenal microsomal and cytosol proteins isolated from animals which received ACTH were significantly lower than those from untreated control animals. The results obtained in this study seem to indicate that the microsomal proteins are one of the major endogenous substrates of the cAMP-dependent protein kinase in rat adrenal glands.