Abstract
The guanine nucleotide-binding regulatory component (G/F) of adenylate cyclase can be purified to homogeneity from rabbit liver and other sources. This protein serves as an essential coupling factor between hormone receptors and the catalytic subunit of the enzyme and is an obligatory activator of the catalyst. The predominant species of G/F behaves as a heterodimer of 35,000– and 45,000–dalton subunits. G/F is a site of action of nonhydrolyzable guanine nucleotide analogs and fluoride; these activators of adenylate cyclase may act by promoting dissociation of the subunits of G/F.
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