Photoaffinity labeling of the beta-adrenergic receptor.
作者： T.N. Lavin , S.L. Heald , P.W. Jeffs , R.G. Shorr , R.J. Lefkowitz
DOI: 10.1016/S0021-9258(19)68497-8
关键词:
摘要: A new photoactive beta-adrenergic antagonist, p-azidobenzylcarazolol (pABC) has been synthesized by combining a carbazole moiety with p-azido-benzyl substituent. The compound labeled tritium to specific activity of 26 Ci/mmol. In frog erythrocyte membranes, [3H]p-azido-benzylcarazolol binds the receptor expected beta 2 specificity and high affinity (KD congruent 100 +/- 10 pM). Unlabeled p-azido-benzylcarazolol can irreversibly inactivate [3H]dihydroalprenolol-binding membranes in photodependent manner which be prevented agents. Incubation or digitonin-solubilized preparations these had enriched receptors Sepharose-alprenolol chromatography step led covalent incorporation radioactivity into Mr = 58,000 peptide. Specific [3H]pABC peptide could both agonists antagonists. This previously purified shown contain receptor-binding site (Shorr, R. G. L., Lefkowitz, J., Caron, M. (1981) J. Biol. Chem. 256, 5820-5826). Thus, photoaffinity labeling protein directly identifies same hormone-binding subunit as isolated conventional purification techniques.
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