Abstract
Publisher Summary This chapter discusses the purification procedures and properties for dog kidney cAMP phosphodiesterase. This enzyme shows an apparent K m for cAMP as substrate in the micromolar range, whereas cGMP is a poor substrate and will inhibit cAMP hydrolysis only at very high concentration. Dog, pig, and rat kidneys contain a similar enzyme and the properties of the purified canine kidney enzyme are similar to those reported for type IV phosphodiesterase (PDE) for lung and skeletal muscle. In contrast to these tissues, liver, heart, and platelet enzymes demonstrate cGMP inhibition of cAMP hydrolysis at low substrate or inhibitor concentrations. The chapter shows differences in the sensitivity of the kidney type IV enzyme to pharmacological inhibitors as compared to effects on the liver type IV activity. The comparative effects of drugs, the relative effects of cGMP to inhibit cAMP hydrolysis, or the ratio of cGMP to cAMP hydrolysis can be used to identify, characterize, and monitor type IV activity during purification.
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