Abstract
Abstract—The protein kinase which in rat brain synaptosomal plasma membranes is responsible for the phosphorylation of a protein band B‐50 (MW 48, 000) was inhibited by the behaviorally active peptide ACTH1–24 and not stimulated by cAMP. Treatment with 0.5% Triton X‐100 in 75 mM‐KCl solubilized 15% of the total B‐50 protein kinase activity and preserved the sensitivity of the enzyme to ACTH1–24. The rate of endogenous phosphorylation of protein band B‐50 was different in intact SPM, solubilized fraction and residue. cAMP stimulated the endogenous phosphorylation of the solubilized fraction in a rather general manner. The solubilized membrane material also phosphorylated B‐50 proteins which were previously extracted from membranes. Column chromatography of the solubilized material over DEAE‐cellulose pointed to the presence of multiple protein kinase activities from rat brain synaptosomal plasma membranes, one of which was the ACTH‐sensitive B‐50 protein kinase.
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