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 language||English (US)|
|Number of pages||4|
|State||Published - Dec 1972|
ASJC Scopus subject areas
- Cancer Research