Abstract
Membranes of mouse L cells that contain adenylate cyclase [ATP pyrophosphate-lyase (cyclizing), EC 4.6.1.1] but lack .beta.-adrenergic receptors were solubilized with Lubrol 12A9. Addition of such adenylate cyclase-containing extracts to .beta.-adrenergic receptor-replete membranes from adenylate cyclase-deficient S49 lymphoma cells resulted in the production of a catecholamine-sensitive adenylate cyclase system. The effects of .beta.-adrenergic agonists and antagonists on the reconstituted system reproduce those that are characteristic of the wild-type S49 lymphoma cell. The uncoupled variant of the S49 lymphoma contained adenylate cyclase, but donor extracts from this clone failed to reconstitute the hormone-sensitive enzyme activity when added to adenylate cyclase-deficient membranes. The uncoupled and adenylate cyclase-deficient variants of the S49 cell are not complementary.