title: The regulatory component of adenylate cyclase from uncoupled S49 lymphoma cells differs in charge from the wild type protein.
abstract: The uncoupled (UNC) variant of the S49 lymphoma possesses the components known to be required for a hormone-sensitive adenylate cyclase system, including receptors for hormones, a guanine nucleotide-binding regulatory protein (G/F), and a catalyst; however, hormones are ineffective in stimulating enzymatic activity in these cells. Two proteins (Mr = 45,000 and 55,000) are labeled with [32P]NAD when wild type or UNC membranes are incubated with the labeled nucleotide and cholera toxin (Johnson, G.L., Kaslow, H.R., and Bourne, H.R. (1978) J. Biol. Chem. 253, 7120-7123). The 45,000-dalton component appears to be a constituent of G/F. Two dimensional electrophoresis of the labeled proteins reveals that both are more acidic when derived from UNC cells.
mesh_terms: D000262:Adenylyl Cyclases / Q000378:metabolism*; D000818:Animals; D002772:Cholera Toxin; D002999:Clone Cells; D014644:Genetic Variation; D008223:Lymphoma / Q000201:enzymology*; D051379:Mice; D008970:Molecular Weight; D009154:Mutation
chemical_list: D002772:Cholera Toxin; D000262:Adenylyl Cyclases