Interactions of pure βγ‐subunits of G‐proteins with purified β1‐adrenoceptor

FEBS Letters

Helmreich, Ernst J.M.¹  Im, Mie-Jae¹  Pfeuffer, Thomas¹  Böttinger, Heiner¹  Holzhöfer, Andreas¹ 

[1] Department of Physiological Chemistry, University of Würzburg, Medical School, D-8700 Würzburg, FRG

关键词: β1-Adrenoceptor;    G-protein;    βγ-subunit;    Protein-protein interaction;    β1AR;    β1-adrenoceptor;    G-proteins;    guanine nucleotide-binding proteins;    Gs;    Gi;    stimulatory and inhibitory guanine nucleotide-binding proteins of adenylyl cyclase;    respectively;    Go;    guanine nucleotide-binding protein first found in brain;    Gn;    guanine nucleotide-binding protein purified from bovine neutrophils Gt;    transducin;    a guanine nucleotide-binding protein purified from rod outer segments;    guanosine-5′-O-3-thiophosphate;    guanosine-5′-O-3-thiophosphate;    GTP;    guanosine-5′-triphosphate;    DTT;    1;    4-dithiothreitol;    [3H]DHA;    [3H]dihydroalprenolol;    cmc;    critical micelle concentration;    PAGE;    polyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(88)80903-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The role of the βγ-subunits in the interaction of G-proteins was examined with β₁-adrenoceptors purified from turkey erythrocytes and pure βγ-subunits prepared from turkey erythrocytes and bovine brain. On a non-denaturing polyacrylamide gel, the mobility of βγ-subunits was increased when incubated with β₁-adrenoceptor and the β₁-adrenergic agonist l-(−)-isoproterenol, whereas on incubation with the antagonist l-alprenolol the mobility was unchanged. Furthermore, the β₁-adrenoceptor was retarded on a Sephadex G-50 column equilibrated with βγ-subunits and agonist. No retardation occurred in the presence of antagonist. These data suggest a direct interaction of activated β₁-adrenoceptors with isolated βγ-subunits of G-proteins.

【 授权许可】

Unknown