Abstract
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.
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