Abstract
The effect of highly purified bovine cytosolic adrenal cortical protein kinase isozyme II catalytic subunit (ATP: Protein Phosphotransferase EC 2.7.1.37) on the formation of pregnenolone from cholesterol in rat and bovine adrenal mitochondrial extracts has been investigated. No stimulation was observed although a low level incorporation of [ 32P] from [ 32P]-ATP into a component or components of the extract was detected. The mitochondrial extracts contained alkaline phosphatase activity that was inhibited by L-cysteine and dithiothreitol. It is concluded that the acute stimulation by ACTH of corticoid production in the rat adrenal does not involve protein kinase mediated phosphorylation of a component or components of the cholesterol sidechain cleavage mixed-function oxygenase system.
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