Abstract
This article describes a new immunopurification procedure based on monoclonal antibodies raised against peptides of the carboxy-terminal region of the turkey β-adrenergic receptor. This procedure constitutes a significant purification step of recombinant β-adrenergic receptors expressed in baculovirus-infected Sf9 cells, and allows the recovery of receptors able to activate Gs in phospholipid vesicles. Additionally, this procedure can be combined with affinity chromatography to yield nearly homogeneous receptor.
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