Reversible Dissociation of Chick Oviduct Progesterone Receptor Subunits

  • Wayne W. Grody
  • William T. Schrader
  • Bert W. O’Malley
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 205)


Previous studies in our laboratory have shown that chick oviduct cytosol contains two 4S progesterone-binding components of different molecular weights, designated A and B, which exhibit high affinity for DNA and chromatin, respectively (Schrader et al., 1972). Both are single polypeptide chains with kinetically identical hormone binding sites (Schrader and O’Malley, 1972). Their molecular weights are 79,000 and 108,000, respectively (Coty et al., 1979; Kuhn et al., 1975). We have postulated that the native cytoplasmic receptor form, sedimenting at 6–8S in low-salt sucrose gradients and containing equal amounts of A and B (Schrader et al., 1975), is a dimer or higher aggregate consisting of one part each of the A and B proteins as subunits.


Progesterone Receptor Sucrose Gradient Native Aggregate Input Ratio Cibacron Blue F3GA 
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Copyright information

© Plenum Press, New York 1986

Authors and Affiliations

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

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