Thermodynamic analysis of isoproterenol binding to beta-adrenoceptors in rat lung membranes.

The thermodynamic properties of the binding of the beta-adrenoceptor agonist isoproterenol and of the antagonist propranolol to beta-adrenoceptors of rat lung were investigated. We found that in our experimental conditions, the high- and low-affinity binding sites for the agonist displayed different properties: the binding to the high-affinity binding site was entropy-driven with a small increase in enthalpy, while agonist binding to the low-affinity binding site was enthalpy-driven. Binding of isoproterenol in the presence of GTP or its non-hydrolyzable analogue GppNHp, and the binding of propranolol were enthalpy-driven with a small increase in entropy.