Reconstitution of a hormone-sensitive adenylate cyclase system. The pure beta-adrenergic receptor and guanine nucleotide regulatory protein confer hormone responsiveness on the resolved catalytic unit.

@article{Cerione1984ReconstitutionOA,
  title={Reconstitution of a hormone-sensitive adenylate cyclase system. The pure beta-adrenergic receptor and guanine nucleotide regulatory protein confer hormone responsiveness on the resolved catalytic unit.},
  author={Richard A. Cerione and David R. Sibley and Juan Codina and Jeffrey L. Benovic and John Winslow and Eva J. Neer and Lutz Birnbaumer and Marc G. Caron and Robert J Lefkowitz},
  journal={The Journal of biological chemistry},
  year={1984},
  volume={259 16},
  pages={9979-82}
}
A hormone responsive adenylate cyclase has been reconstituted in phosphatidylcholine vesicles from its isolated protein components. The proteins used were the affinity chromatography purified (500-2000-fold) or pure Mr = 64,000 beta-adrenergic receptors (beta AR) isolated from hamster and guinea pig lung membranes, the pure heterotrimeric (Mr: alpha = 42,000; beta = 35,000; gamma approximately equal to 5,000) guanine nucleotide regulatory protein (Ns) isolated from human erythrocyte membranes… CONTINUE READING