Erneux C, Miot F, Van Haastert P J, Jastorff B
J Cyclic Nucleotide Protein Phosphor Res. 1985;10(5):463-72.
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.
通过添加浓度递增的未标记的环磷酸腺苷（cAMP）和环磷酸鸟苷（cGMP）类似物，研究了[3H]cGMP与纯化的牛肾上腺cGMP刺激的磷酸二酯酶的结合特异性。数据表明，cAMP磷酸二酯酶活性的刺激效力与[3H]cGMP结合的置换曲线之间存在完美的相关性。由于3',5'-单磷酸腺苷的Sp和Rp非对映异构体分别表现为cAMP依赖性蛋白激酶激动剂和拮抗剂，因此研究了这些化合物以及相应的cGMP类似物（cGMPS Sp和Rp）对cGMP刺激的磷酸二酯酶可能的生物学活性。数据表明，在结合或激活两种（Sp）或（Rp）异构体之一方面不存在区域选择性。
