Resolution of some components of adenylate cyclase necessary for catalytic activity

E. M. Ross, A. G. Gilman

Research output: Contribution to journalArticle

130 Scopus citations

Abstract

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 languageEnglish (US)
Pages (from-to)6966-6969
Number of pages4
JournalJournal of Biological Chemistry
Volume252
Issue number20
StatePublished - Dec 1 1977

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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