Adenylate cyclase activity in a Lubrol 12A9 extract of wild type S49 lymphoma plasma membranes is completely inactivated by incubation at 37° for 20 min. Activity is restored by mixing this heated extract of wild type membranes with an unheated detergent extract of membranes from a variant clone that lacks measureable adenylate cyclase activity (AC-). The factor(s) donated by the AC- extract is labile to heating at 30° (t(1/2) = 3 min) or to treatment with N-ethylmaleimide or trypsin. The factor(s) donated by the heated wild type extract is also sensitive to proteases or N-ethylmaleimide. This extract displays more complex inactivation kinetics at 50°, consistent with the existence of separate factors necessary for the stimulatory effects of NaF and guanyl-5'-yl-imidodiphosphate. It is suggested that at least 2 proteins are necessary for adenylate cyclase activity and that one of these is retained in the phenotypically adenylate cyclase-deficient variant.
|Original language||English (US)|
|Number of pages||4|
|Journal||Journal of Biological Chemistry|
|State||Published - Dec 1 1977|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology