Cyclic AMP phosphodiesterases of the rat ovary. Oestrous cycle dependent activity change of high affinity form.

In the rat ovary, from prenatal to adult stages, two electrophoretically distinct forms of cyclic AMP phosphodiesterase (E.C.: 3.1.4.17) occur. These forms were analysed for their affinity towards cAMP in both crude and partially purified preparations. Whereas the slow electrophoretic form, which has a low affinity towards cAMP, shows a linear Lineweaver-Burk plot, the fast electromorph exhibits anomalous kinetic behaviour in that cAMP affinity appears to increase with decreasing cAMP-concentration. This form shows dramatic alteration of maximum velocity during the oestrous cycle, attaining maximum activity at metoestrus. This rise of activity is sensitive to inhibition of protein synthesis.