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The regulatory component of adenylate cyclase from uncoupled S49 lymphoma cells differs in charge from the wild type protein

Schleifer, L S ; Garrison, J C ; Sternweis, P C ; Northup, J K ; Gilman, A G

The Journal of biological chemistry, 1980-04, Vol.255 (7), p.2641-2644 [Periódico revisado por pares]

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Título:
The regulatory component of adenylate cyclase from uncoupled S49 lymphoma cells differs in charge from the wild type protein
Autor: Schleifer, L S ; Garrison, J C ; Sternweis, P C ; Northup, J K ; Gilman, A G
Assuntos: Adenylyl Cyclases - metabolism ; Animals ; Cholera Toxin ; Clone Cells ; Genetic Variation ; Lymphoma - enzymology ; Mice ; Molecular Weight ; Mutation
É parte de: The Journal of biological chemistry, 1980-04, Vol.255 (7), p.2641-2644
Descrição: 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.
Editor: United States: American Society for Biochemistry and Molecular Biology
Idioma: Inglês

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