Biochemical characterization of phosphorylated .beta.-adrenergic receptors from catecholamine-desensitized turkey erythrocytes

Isoproterenol-induced desensitization of turkey erythrocyte adenylate cyclase is accompanied (1) by a decrease in the mobility of beta-adrenergic receptor proteins, specifically photoaffinity labeled with 125I-(p-azidobenzyl)carazolol (125I-PABC), on sodium dodecyl sulfate (SDS)-polyacrylamide gels...

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Veröffentlicht in:	Biochemistry (Easton) 1986-06, Vol.25 (12), p.3719-3724
Hauptverfasser:	Stadel, Jeffrey M, Rebar, Richard, Shorr, Robert G. L, Nambi, Ponnal, Crooke, Stanley T
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acids - analysis Animals beta -adrenergic Biological and medical sciences catecholamines Cell receptors Cell structures and functions Erythrocyte Membrane - metabolism erythrocytes Fundamental and applied biological sciences. Psychology Hydrolysis Iodine Radioisotopes Isoproterenol - pharmacology Molecular and cellular biology Phosphorus Radioisotopes Phosphorylation Receptors, Adrenergic, beta - drug effects Receptors, Adrenergic, beta - isolation & purification Receptors, Adrenergic, beta - metabolism Turkeys
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