The dioxin receptor: Characterization of its DNA-binding properties

Grant G.F. Mason, Anna Wilhelmsson, Scott Cuthill, Mikael Gillner, Lorenz Poellinger, Jan Åke Gustafsson

Research output: Contribution to journalArticlepeer-review

4 Scopus citations


The binding of the rat hepatic dioxin and glucocorticoid receptors to the polyanionic matrices heparin-Sepharose and DNA-cellulose in virto and to cell nuclei in vivo was studied under various conditions. In a non-liganded and non-activated state both receptors eluted from heparin-Sepharose at a low ionic strength and were not retained on DNA-cellulose. Following ligandation and activation in virto both receptors showed an increased affinity for heparin-Sepharose and were retained on DNA-cellulose. In analogy to these in virto data, it was found that a high salt concentration (0.4 M KCl) was required to extract in vivo liganded dioxin receptor from purified nuclear preparations in contrast to that previously reported for non-liganded nuclear receptors. Limited proteolysis of both dioxin and glucocorticoid receptors resulted in molecular species of similar binding properties with regard to DNA-cellulose and heparin-Sepharose. We conclude that, in addition to the dioxin and glucocorticoid receptors showing considerable similarities in their physicochemical properties, they may also share a similar structural organization with regard to functional domains.

Original languageEnglish (US)
Pages (from-to)307-310
Number of pages4
JournalJournal of Steroid Biochemistry
Issue number1-6
StatePublished - 1988

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology


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