[Properties of 3':5'-AMP- and 3':5'-GMP-phosphodiesterases in the retina].

The activity of 3':5'-AMP and 3':5'-GMP phosphodiesterase was determined in retina of some animals. In all cases the enzymic activity with the presence of 3':5'-GMP is higher than with utilization of 3':5'-AMP. About 60% of the enzyme activity with 3':5' GMP as a substrate is lost in the process of obtaining the outer segments extracted from the bovine retina. The enzyme activity was completely detected with 3':5' AMP as a substrate. The both enzymes are equally extracted from the photoreceptory membranes by a weak ionic buffer. Differences are found in the stability of 3':5'-AMP and 3':5-GMP-phosphodiesterase during storage. The form of the enzyme splitting 3':5'-GMP is more unstable.