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Research Article

Identification of a Large form of the Chick Liver Estrogen Receptor

Pages 317-330 | Published online: 26 Sep 2008

References

  • Deeley R. G., Gordon J. I., Burns A. T., Mullinix K. P., Binastein M., Goldberger R. F. Primary activation of the vitellogenin gene in the rooster. J. Biol. Chem. 1977; 252: 8310–8319
  • Mester J., Baulieu E -E. Nuclear estrogen receptor of chick liver. Biochem. Biophys. Acts. 1977; 261: 236–244
  • Lebeau M -C, Massol N., Baulieu E -E. An insoluble receptor for oestrogens in the “residual” nuclear protein of chick liver. Eur. J. Biochem. 1973; 36: 294–300
  • Gschwendt M., Kittstein W. Specific binding of estradiol to the liver chromatin of estrogenized roosters. Biochem. Biophys. Acta. 1974; 361: 84–96
  • Gswendt M. Solubilization of the chromatin-bound estrogen receptor from chick liver and fractionation on hydroxyl-apatite. Eur. J. Biochem. 1976; 67: 411–419
  • Schneider W., Gswendt M. Kinetics of the appearance of nuclear estrogen binding sites in chicken liver. Hoppe-Seyler's Z. Physiol. Chem. 1977; 358: 1583–1589
  • Arias F., Warren J. C. An estrophilic macromolecule in chick liver cytosol. Biochem. Biophys. Acta. 1971; 230: 550–559
  • Lazier C., Alford W. S. Interaction of the anti-oestrogen, nafoxidine hydrochloride, with the soluble nuclear oestradiol-binding protein in chick liver. Biochem. J. 1977; 164: 659–667
  • Gswendt M. A cytoplasmic high affinity estrogen-binding protein in the embryonic chick liver. Eur. J. Biochem. 1977; 80: 461–468
  • Lazier C. B., Haggarty A. J. A high-affinity oestrogen-binding protein in cockerel liver cytosol. Biochem. J. 1979; 180: 347–353
  • Nielsen C. J., Vogel W. M., Pratt W. B. Inactivation of glucocorticoid receptors in cell free preparations of rat liver. Cancer Res. 1977; 37: 3420–3426
  • Toft D., Nishigori H. Stabilization of the avian progesterone receptor by inhibitors. J. Steroid Biochem. 1979; 11: 413–416
  • Nishigori H., Toft D. Inhibition of progesterone receptor activation by sodium molybdate. Biochemistry 1980; 19: 77–83
  • Wolfson A., Mester J., Yang C -R, Baulieu E -E. “Non-activated” form of the progesterone receptor from chick oviduct: characterization. Biochem. Biophys. Res. Comm. 1980; 95: 1577–1584
  • Miller L. K., Tuazon F. B., Niu E -M, Sherman M. R. Human breast tumor estrogen receptor: effects of molybdate and electrophoretic analyses. Endocrinology 1981; 108: 1369–1378
  • Mester J., Renoir J -M, Yang C -R, Wolfson A., Baulieu E -E. Characterization of “native” and “activated” progesterone and oestrogen receptors from chick oviduct cytosol. Mechanism of Steroid Hormone Action, J. Lewis, M. Ginsburg, London, (in press)
  • Martin R. G., Ames B. N. A method for determining the sedimentation behavior of enzymes: application to protein mixtures. J. Biol. Chem. 1961; 236: 1372–1379
  • Siegel L. M., Monty K. J. Determination of molecular weights and frictional ratios of proteins in impure systems by use of gel filtration and density gradient centrifugation. Biochem. Biophys. Acta. 1966; 112: 346–362
  • Molinari A. M., Medici N., Moncharmont B., Puca A. Estradiol receptor of calf uterus: interaction with heparin-agarose and purification. Proc. Natl. Acad. Sci. USA 1977; 74: 4886–4890
  • Sutherland R. L., Baulieu E -E. Quantitative estimates of cytoplasmic and nuclear oestrogen receptors in chick oviduct. Eur. J. Biochem. 1976; 70: 531–541
  • Schrader W. T., Heuer S. S., O'Malley B. W. Progesterone receptors of chick oviduct: identification of 6S receptor dimers. Biol. Reprod. 1975; 12: 134–142

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