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A comparison of the binding characteristics of the beta-adrenoceptor antagonists 3H-dihydroalprenolol and 125I-iodocyanopindolol in rat liver.

The binding characteristics of 3H-dihydroalprenolol and 125I-iodocyanopindolol have been compared in a particulate fraction from regenerating rat liver. When total 3H-dihydroalprenolol binding and inhibition of total 3H-dihydroalprenolol binding by (-)isoprenaline, (-)alprenolol and (+/-)cyanopindolol was investigated, it was found that all agents were bound to two classes of saturable binding sites. In the inhibition studies, the presence of two binding components was not obvious until the data were transformed into Hofstee plots and these were decomposed, except in the case of (+/-)cyanopindolol. Only (+/-)cyanopindolol was found to distinguish clearly between the two saturable binding sites identified by 3H-dihydroalprenolol, as indicated by a broad plateau in the inhibition curve. When 125I-iodocyanopindolol was used as radioligand, only one saturable binding site was identified, even in the presence of less selective inhibiting ligands. The lower affinity component of 3H-dihydroalprenolol binding could be inhibited by 10 microM phentolamine. However, binding experiments with 3H-prazosin indicated that the lower affinity component was not identical with the alpha-adrenoceptor. Phentolamine did not influence 125I-iodocyanopindolol binding. Thus, due to its higher specific activity and a high degree of selectivity, 125I-iodocyanopindolol appears to be the ligand of choice.