Progesterone Receptors of Chick Oviduct

  • William T. Schrader
  • Bert W. O’Malley
Chapter
Part of the Advances in Experimental Medicine and Biology book series (AEMB)

Abstract

The chick oviduct progesterone receptor has been purified to homogeneity by affinity chromatography and its molecular action studied in vitro. The native receptor is a 200,000 MW dimer of two dissimilar 4S subunits with different intranuclear function. The receptors directly regulate RNA chain initiation sites in oviduct chromatin by interactions involving target tissue nuclear acceptor sites. There is a 1:1 correspondence between receptor “acceptor” sites and RNA sites. Only the dimer form of the receptor is active in vitro on chromatin templates. The study suggests a novel model for hormone action which can be tested directly in this system.

Keywords

Progesterone Receptor Initiation Site Ammonium Sulfate DEAE Cellulose Average Chain Length 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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Copyright information

© Springer Science+Business Media New York 1978

Authors and Affiliations

  • William T. Schrader
    • 1
  • Bert W. O’Malley
    • 1
  1. 1.Department of Cell BiologyBaylor College of MedicineHoustonUSA

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