ABSTRACT
A principle tenet in pharmacology is that neurotransmitters, drugs, and hormones interact with specific receptor sites to produce or inhibit a characteristic physiological response. In the case of synaptic transmission and many hormone responsive systems, these specific receptor sites are presumed to be integral membrane proteins. The purification folds obtained by the methods represent a 6500-fold purification from initial detergent extracts and a greater than 80000-fold purification from membrane preparations. As the techniques were found to be extremely successful for the purification of the β2-adrenergic receptor, we sought to purify the β1-adrenergic receptor from the turkey red blood cell. Purification and characterization of hormone and drug receptors has been a difficult task primarily due to the extremely small quantities of these macromolecules in most cell types. β-Adrenergic receptors are closely coupled to the enzyme adenylate cyclase and have been the focus of considerable attention.
