Inhibition of Protein Kinase C from Polymorphonuclear Neutrophils by Long Chain Acyl Coenzyme A and Counteraction by Mg-ATP

The Ca2+- and phospholipid-dependent protein kinase (protein kinase C) from bovine polymorphonuclear neutrophils was inhibited by micromolar amounts of long chain acyl-CoAs. The extent of inhibition at a given concentration of the acyl-CoAs depended on the length of the chain. A chain length of at least 12C was required for inhibition. Inhibition of protein kinase C activity was counteracted specifically by Mg-ATP.