Interaction of the hepatic receptor protein for 2,3,7,8-tetrachlorodibenzo-p-dioxin with DNA

Jan M.B. Carlstedt-Duke, Ulla Britt Harnemo, Bertil Högberg, Jan Åke Gustafsson

Research output: Contribution to journalArticlepeer-review

31 Scopus citations

Abstract

2,3,7,8-Tetrachlorodibenzo-p-dioxin (TCDD) binds to a specific, high-affinity, low-capacity protein in rat liver cytosol. The TCDD-receptor complex is a large molecule with a Stokes radius of 6.6 nm as determined by gel filtration on calibrated columns. The receptor complex sediments at 5.0 S on glycerol gradients. The calculated molecular weight from the physical parameters was 136 000 and the frictional ratio 1.79. The TCDD-receptor complex binds to DNA-cellulose without preceding heat activation or incubation at high ionic strength. The receptor must first bind TCDD before it can interact with DNA. The DNA-binding ability can be removed from the TCDD receptor by limited proteolysis with trypsin. This treatment does not affect the TCDD-binding site of the receptor. The proteolytic fragment of the TCDD-receptor complex containing the TCDD-binding site but not the ability to bind to DNA appears to be approximately the same size as the native receptor, as judged from chromatography of Sepharose CL-6B and glycerol gradient centrifugation.

Original languageEnglish (US)
Pages (from-to)131-141
Number of pages11
JournalBBA - General Subjects
Volume672
Issue number2
DOIs
StatePublished - Jan 21 1981

Keywords

  • (Rat liver)
  • DNA-receptor interaction
  • Receptor protein
  • Tetrachlorodibenzodioxin

ASJC Scopus subject areas

  • Molecular Biology
  • Biophysics
  • Biochemistry
  • Medicine(all)

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