Partial characterization of [3H]methyltrienolone binding in rat prostate cytosol

Åke Pousette, Marek Snochowski, Dominique Bression, Bertil Högberg, Jan Åke Gustafsson

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13 Scopus citations


3H-labelled R 1881 (methyltrienolone) was bound with high affinity (Kd, 2 · 10-9 M) and low capacity (11-15 fmol/mg protein) in prostate cytosol from rats castrated 18 h earlier. The binding was inhibited by 5α-dihydrotosterone, testosterone, cyproterone acetate and LEO 1727, but not by estradiol-17β, R 5020 or corticosterone. The 3H-labelled R 1881-receptor complex was excluded from a Sephadex G-200 column, had a sedimentation coefficient of 3.5 S, was eluted from a DEAE-cellulose column at 0.2 M KCl concentration and precipitated between 20-40% of saturation of ammonium sulfate. 20% of specifically bound 3H-labelled R 1881 was retained by DNA-cellulose at low ionic strength. The fraction which was not bound to DNA-cellulose did not bind either, after rechromatography, not even following heating at 20°C for 20 min or following fractionation with ammonium sulphate. In summary, the results indicate that the 3H-labelled R 1881-receptor complex in rat prostate cytosol has characteristics similar to those of the 5μ-[3H]-dihydrotestosterone-receptor complex.

Original languageEnglish (US)
Pages (from-to)358-367
Number of pages10
JournalBBA - General Subjects
Issue number2
StatePublished - Jan 18 1979


  • (Rat prostate)
  • Androgen receptor
  • Methyltrienolone

ASJC Scopus subject areas

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


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