Transformation of human progesterone receptor in the presence of the progestin (R5020) and the antiprogestin (RU486).

@article{Miller1988TransformationOH,
  title={Transformation of human progesterone receptor in the presence of the progestin (R5020) and the antiprogestin (RU486).},
  author={Marilyn M. Miller and Clement Hurd and Virinder K. Moudgil},
  journal={Journal of steroid biochemistry},
  year={1988},
  volume={31 5},
  pages={
          777-83
        }
}
We have examined and compared the binding characteristics and transformation in vitro of human uterine cytosolic progesterone receptor (PR) bound to either the progestin agonist, R5020 or the antiprogestin, RU486. Incubation of cytosol with 5-20 nM [3H]R5020 and [3H]RU486 yielded macromolecular complexes that sedimented in the 4S and 8S regions in 10-35% glycerol gradients. The 8S peaks of radioactivity due to macromolecular-bound [3H]R5020 or [3H]RU486 could be eliminated by a preincubation of… CONTINUE READING