The beta-adrenergic receptor survives solubilization in deoxycholate while forming a stable association with the agonist.

Agonist, but not antagonist, protects the beta-adrenergic receptor from inactivation during solubilization in deoxycholate. Protection is apparently due to locking of the agonist in the receptor, a high affinity interaction induced or stabilized by this detergent. The guanyl nucleotide-binding protein which normally interacts with the receptor to induce high affinity binding of the hormone is apparently not required in this agonist-specific locking process. It is therefore possible that deoxycholate mimics the effect of the guanyl nucleotide-binding protein on the conformation of the hormone-occupied receptor. The experiments further show that the receptor in deoxycholate is quite stable for days, provided that it is occupied by the agonist. Removal of deoxycholate brings about the release of the locked agonist and the return of the receptor to the dynamic functional state.