The subunits of G family G proteins, G(G), G(G), and G were expressed with G protein and subunits in insect cells using a baculovirus system. The trimeric forms of G proteins, G (G), G (G), and G (G), were solubilized by 1% sodium cholate and purified by sequential chromatography on three kinds of columns. G, G, and G activated phospholipase C- purified from bovine brain in the presence of aluminum fluoride to the same extent. Muscarinic acetylcholine receptor m1 subtype stimulated the guanosine 5`-O-(3-thiotriphosphate) (GTPS) binding to G, G, and G in the presence of similar concentrations of carbamylcholine. When m1 receptor, G protein, and phospholipase C- were reconstituted in lipid vesicles, each subtype of G family G proteins mediated the activation of phospholipase C- by carbamylcholine in the presence of either 1 µM GTPS or 1 mM GTP. Phospholipase C- stimulated the GTPase activity of G, G, and G in the presence of m1 receptor and carbamylcholine but did not stimulate the GTPase activity of G. Protein kinase C phosphorylated m1 receptor and phospholipase C-, but the phosphorylation did not significantly affect the ability of the m1 receptor to stimulate phospholipase C- in the reconstitution system of purified proteins.

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