ATP-dependent enzyme activating hormone binding of estradiol receptor

F. Auricchio, A. Migliaccio, G. Castoria, S. Lastoria, E. Schiavone

Research output: Contribution to journalArticlepeer-review


Mouse uterus estradiol receptor undergoes a inactivation-reactivation process "in vitro". The specific estrogen binding activity inactivated by nuclei, apparently through a dephosphorylation process (1,2,3), is reactivated by an ATP-dependent process. The enzyme reactivating the receptor has been purified from calf uterus cytosol. It shows high affinity for the inactive receptor (Km of ∼ 0.3 × 10-9 mol of 17β-estradiol binding sites/l); it is simulated by MgCl2 and CaCl2. Present and previous results suggest that in cytoplasm of intact cells a phosphorylation process makes the receptor able to bind hormone and in nuclei dephosphorylation of receptor causes loss of hormone binding activity.

Original languageEnglish
Pages (from-to)1171-1178
Number of pages8
JournalBiochemical and Biophysical Research Communications
Issue number4
Publication statusPublished - Aug 31 1981

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology


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