Solubilization of glucagon and epinephrine sensitive adenylate cyclase from rat liver plasma membranes

Hormonally sensitive adenylate cyclase has been solubilized from rat liver plasma membranes using Triton X-305 in Tris buffers containing mercaptoethanol and MgCl 2. The solubilized enzyme was stimulated 5 fold by NaF, 7 fold by glucagon and 20 fold by epinephrine. Criteria for solubilization included lack of sedimentation at 100,000 × g for one hour, the absence of particulate material in the 100,000 × g supernatant when examined by electron microscopy, and inclusion of hormonally sensitive adenylate cyclase activity in Sephadex G 200 gels. The molecular weight of the solubilized, hormonally sensitive enzyme was approximately 200,000 in the presence of Triton X-305.