Separation of glucocorticoid receptors by phosphocellulose chromatography at pH 6.8

James S. Norris, Peter O. Kohler

Research output: Contribution to journalArticle

1 Scopus citations

Abstract

A high molecular weight glucocorticoid receptor partially purified at pH 7.4 from DDT, MF-2 cytosol in the presence of sodium molybdate can be shown to elute from DEAE-cellulose at 0.20 M KCl. This receptor fails to bind to phosphocellulose. However, if the receptor is partially purified at pH 6.8 it now binds to phosphocellulose eluting at 0.14 M KCl. A smaller fraction of receptor obtained at pH 6.8 elutes from phosphocellulose at 0.21 M KC1 and from DEAE-cellulose at 0.09 M KCl. Neither of the two receptor forms binds to DNA-cellulose unless a heating step (30° for 15 min) in the absence of sodium molybdate is performed. Under these conditions the form eluting at 0.09 M (DEAE) or 0.21 M KCl (phosphocellulose) is transformed to a DNA-binding form. Concomitant with transformation is a shift in sedimentation velocity from 8.8S to 3.9S.

Original languageEnglish (US)
Pages (from-to)337-341
Number of pages5
JournalJournal of Steroid Biochemistry
Volume15
Issue numberC
DOIs
StatePublished - Dec 1981

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology

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