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Adenosine 3',5'-cyclic monophosphate (cAMP) phosphodiesterase activity in crude guinea-pig superior cervical ganglion homogenates was assayed under a variety of experimental conditions. Two forms of cAMP phosphodiesterase were found, one with high and the other with low affinity for the substrate. The Km values were about 1 and 110 microM respectively. Imidazole slightly but constantly stimulated the former enzyme form over a wide range of concentrations and 1-methyl-3-isobutylxanthine was a weak competitive inhibitor with a Ki value of 90 microM. Low affinity cAMP phosphodiesterase activity was increased by calmodulin and Ca2+. This stimulation was not observed in the presence of trifluoperazine, a specific inhibitor of calmodulin. On the other hand, neither [D-Ala2]met-enkephalinamide nor prostaglandin E2, alone or in combination, influenced high affinity cAMP phosphodiesterase.
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