cAMP-dependent protein kinase from Mucor rouxii: Physical evidence of a ternary complex holoenzyme-cAMP

R. L. Pastori, N. Kerner, S. Moreno, S. Passeron

Research output: Contribution to journalArticle

11 Scopus citations

Abstract

Gel electrophoresis and sucrose density gradient centrifugation techniques permitted the visualization for the first time of the ternary complex formed by the binding of cAMP to Mucor rouxii cAMP-dependent protein kinase holoenzyme. The addition of 0.5 M NaCl or histone plus ATP-Mg++, together with cAMP, dissociates the holoenzyme into free regulatory (R) and catalytic (C) subunits. At 4°C, cAMP bound to the holoenzyme is readily exchangeable with unlabeled cAMP (half life 2.5 min), while the nucleotide bound to the R subunit has a very slow exchange rate (half life 210 min). The amount of cAMP bound to R subunit is approximately twice the amount bound to holoenzyme at saturation.

Original languageEnglish (US)
Pages (from-to)663-671
Number of pages9
JournalBiochemical and biophysical research communications
Volume101
Issue number2
DOIs
StatePublished - Jul 30 1981
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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