Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 8 October 1976:
Vol. 194. no. 4261, pp. 197 - 199
DOI: 10.1126/science.183267

Articles

Science, Vol 194, Issue 4261, 197-199
Copyright © 1976 by American Association for the Advancement of Science


articles

Progesterone binding to hen oviduct genome: specific versus nonspecific binding

TC Spelsberg, GM Pikler, and RA Webster

Data are presented to explain discrepancies in the literature involving the in vitro binding of steroid receptor complexes to isolated nuclei and chromatin. The type of binding in vitro of the progesterone-receptor complex to nuclei, chromatin, or DNA of hen organs is largely determined by the ionic strength of the medium. Low ionic conditions (0.01 to 0.05 molar potassium chloride) result in a nonspecific, nonsaturable binding, while high ionic conditions (0.15 to 0.20 molar potassium chloride) create a tissue-specific, saturable binding. Pure DNA binds the steroid receptor complex extensively in low salt but very little in the higher salt conditions.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
1 alpha, 25-Dihydroxyvitamin D3 nuclear receptors in pituitary.
H. Gelbard, P. Stern, and D. U'Prichard (1980)
Science 209, 1247-1249
   Abstract »    PDF »



To Advertise     Find Products


Science. ISSN 0036-8075 (print), 1095-9203 (online)