The binding of cyclic nucleotide analogs to a purified cyclic GMP-stimulated phosphodiesterase from bovine adrenal tissue.
The specificity of binding of [3H]cGMP to purified bovine adrenal cGMP-stimulated phosphodiesterase was investigated by adding increasing concentrations of unlabelled analogs of cAMP and cGMP. The data show a perfect correlation between the potencies of stimulation of cAMP phosphodiesterase activity and displacement curves of [3H]cGMP binding. Since the Sp and Rp diastereomers of adenosine 3',5'-monophosphate behaved as a cAMP-dependent protein kinase agonist and antagonist, respectively, the possible biological activity of these compounds and the corresponding cGMP analogs (cGMPS Sp and Rp) on the cGMP-stimulated phosphodiesterase was investigated. The data show no regioselectivity in binding nor on activation of one of the two (Sp) or (Rp) isomers.
D015106:3',5'-Cyclic-GMP Phosphodiesterases / Q000378:metabolism*; D000311:Adrenal Glands / Q000201:enzymology*; D000818:Animals; D002417:Cattle; D006152:Cyclic GMP / Q000031:analogs & derivatives* / Q000378:metabolism*; D007700:Kinetics; D011485:Protein Binding; D013329:Structure-Activity Relationship
D015106:3',5'-Cyclic-GMP Phosphodiesterases; D006152:Cyclic GMP