An aprotinin binding site localized in the hormone binding domain of the estrogen receptor from calf uterus

Vincenzo Nigro, Nicola Medici, Ciro Abbondanza, Saverio Minucci, Bruno Moncharmont, Anna Maria Molinari, Giovanni Alfredo Puca

Research output: Contribution to journalArticlepeer-review

Abstract

It has been proposed that the estrogen receptor bears proteolytic activity responsible for its own transformation. This activity was inhibited by aprotinin. Incubation of transformed ER with aprotinin modified the proteolytic digestion of the hormone binding subunit by proteinase K. The smallest hormone-binding fragment of the ER, obtained by tryptic digestion, was still able to bind to aprotinin. These results suggest that aprotinin interacts with ER and the hormone-binding domain of ER is endowed with a specific aprotinin-binding site.

Original languageEnglish
Pages (from-to)930-936
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume170
Issue number2
DOIs
Publication statusPublished - Jul 31 1990

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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