A Distinction between 3-Methylcholanthrene and Estrogen Binding in the Uterus

D. O. Toft, T. C. Spelsberg

Research output: Contribution to journalArticlepeer-review

14 Scopus citations

Abstract

The binding of methylcholanthrene-3H to macromolecular components of the uterine cytosol fraction was analyzed and compared with the specific binding of estradiol to its receptor. Methylcholanthrene-3H binds to a component which sediments as a 5 S complex on sucrose gradients and can be easily distinguished from the 8 S estradiol-receptor complex. Unlabeled estradiol does not interfere with methylcholanthrene-3H binding, nor does unlabeled methylcholanthrene have any effect on the formation or sedimentation of the estradiol-3H-receptor complex. These results negate the possibility that the carcinogen acts in estrogenic target tissues by directly interfering with the normal interaction of estrogens with their receptor sites.

Original languageEnglish (US)
Pages (from-to)2743-2746
Number of pages4
JournalCancer research
Volume32
Issue number12
StatePublished - Dec 1972

ASJC Scopus subject areas

  • Oncology
  • Cancer Research

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