Isolation of homologous and heterologous complexes between catalytic and regulatory components of adenylate cyclase by forskolin—Speharose

FEBS Letters

Pfeuffer, Thomas²  Metzger, Heinz¹  Gaugler, Bernhard² 

[1] Hoechst Aktiengesellschaft, Frankfurt/Main, FRG;Department of Physiological Chemistry, University of Würzburg, School of Medicine, D-8700 Würzburg, FRG

关键词: Adenylate cyclase;    Forskolin;    G-protein;    Reconstitution;    Guanine nucleotide;    Gpp(NH)p;    guanosine 5′-(β;    γ-imino)triphosphate;    GTPγ;    guanosine 5′-(3-thiotriphosphate);    Mops;    3-(N-morpholino)propanesulfonic acid;   

DOI  :  10.1016/0014-5793(83)80040-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Homologous and heterologous complexes between catalytic and GTP-binding components can be isolated by means of immobilized succinyldeacetylforskolin (forskolin—Sepharose). A heterologous complex is formed by reconstitution of forskolin—Sepharose bound catalytic function from rabbit myocardial membranes with the homogeneous [³H]methyl-GTP-binding protein from duck erythrocyte membranes. Analysis of the reconstituted complex by sodium dodecyl sulfate polyacrylamide gelelectrophoresis reveals that only the M _r 42 000 component of the GTP-binding protein's M _r 42 000/M _r 35 000 heterodimer contributes to the formation of active adenylate cyclase.

【 授权许可】

Unknown