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Properties and cellular distribution of cyclic AMP‐dependent protein kinase from thymus

A protein kinase that catalyzes the phosphorylation of histone was partially purified from rat thymus, and the rate of histone phosphorylation was stimulated three‐ to fourfold by 1 × 10−6 M adenosine 3′,5′‐monophosphate (cyclic AMP). Thymic protein kinase was more active than the enzyme from spleen. Histone fractions f1, f2a, f2b, and f3 were all capable of serving as phosphate acceptors for the thymic protein kinase, and the rate of phosphorylation of each fraction was stimulated by cyclic AMP. The ability of various 3′,5′‐mononucleotides to stimulate protein kinase activity was compared. Inosine 3′,5′‐monophosphate (cyclic IMP) was the most effective substitute for cyclic AMP.