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Protein kinase activity was identified in the nuclear, microsomal, lysosomal-mitochondria1 and soluble fractions isolated from calf ovaries. In all particulate fractions the protein kinase activity was only slightly stimulated by adenosine 3': 5'-monophosphate (CAMP) as compared to a 5-fold stimulation of the soluble kinase activity. More than 80% of the enzyme activity measured in the presence of CAMP was found in the soluble fraction. Incubation with 0.2 % Triton X-100 resulted in a 2 -3-fold increase in the protein kinase activities in the lysosomal-mitochondria1 and microsomal fractions. Triton X-100 solubilized 40 -60

High resolving power and quantitative application of polyacrylamide‐gel electrophoresis at various pore sizes and electrofocusing provide resolution of a calf‐ovarian protein‐kinase system at an increased level of magnification, as well as optimal preparative routes. Three protein kinases dependent on adenosine 3′:5′‐monophosphate are distinguished by polyacrylamide gel electrophoresis in calf ovarian cytosol. These enzymes which are observed in the pH range 7.5–10.2, appear to be aggregates of a common subunit or monomer. The three kinases are, by the criteria of polyacrylamide gel electrophoresis, distinct from three adenosine‐3′:5′‐monophosphate‐binding proteins found in the calf ovarian system. Analysis by electrofocusing on polyacrylamide gel shows that conventionally purified preparations of the major kinase of cytosol contain an overwhelming majority of contaminant proteins.