[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.
D015105:3',5'-Cyclic-AMP Phosphodiesterases / Q000378:metabolism*; D015106:3',5'-Cyclic-GMP Phosphodiesterases / Q000378:metabolism*; D000818:Animals; D001001:Anura; D002417:Cattle; D010856:Columbidae; D005399:Fishes; D007798:Lampreys; D011817:Rabbits; D011896:Rana temporaria; D051381:Rats; D012160:Retina / Q000201:enzymology*; D013045:Species Specificity
D015105:3',5'-Cyclic-AMP Phosphodiesterases; D015106:3',5'-Cyclic-GMP Phosphodiesterases
Svoĭstva 3':5'-AMP- i s':5'-GMP-fosfodiésteraz v setchatke.