Abstract
Removal of contaminating proteins from rat ovarian cytosol by DEAE chromatography results in a 358% recovery of protein kinase C activity. The data suggest that rat ovaries contain an endogenous inhibitor of protein kinase C whose activity dominates that of protein kinase C in the cytosol. The inhibitor is specific for protein kinase C and does not activate the enzyme through proteolysis. This endogenous inhibitor may be important in the hormonal control of protein kinase C in the rat ovary, and may become an important tool in the study of the role of protein kinase C in other cell functions.
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