The Protein Journal

, Volume 23, Issue 7, pp 461–465 | Cite as

Radiation Inactivation Analysis of Progesterone Receptor in Human Uterine Cytosol

  • Chi-ming Wu
  • Tse-jia Liu
  • Ling-ling Hsieh
  • Rong-long Pan


It is believed that human progesterone receptor (PR) contains a ligand binding subunit A (83 kDa) or subunit B (120 kDa) and 2 copies of heat shock proteins (hsp90) of molecular weight 90 kDa. To elucidate the mechanism of hormone binding, we employed radiation inactivation to determine its functional size. The functional masses determined in the presence of glycerol, molybdate and potassium chloride were 120 \pm 14, 124 \pm 13 and 130 \pm 20 kDa, respectively. From scatchard plot analysis, the radiation decreased the binding sites and increased the binding affinity of PR with ligand. The functional masses of PR dissolved in the three variant buffers were similar to the molecular weight of PR subunit B. The results implied that PR subunit B could bind with ligand despite hsp90 and hsp90 was not involved in the PR binding to progesterone.


Functional size Progesterone receptor radiation inactivation 



ethylendiaminetetraacetic acid


90 kDa heat shock protein


progesterone receptor




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Copyright information

© Springer Science+Business Media, Inc. 2004

Authors and Affiliations

  • Chi-ming Wu
    • 1
  • Tse-jia Liu
    • 2
  • Ling-ling Hsieh
    • 1
  • Rong-long Pan
    • 3
  1. 1.Graduate Institute of Basic Medical ScienceChang Gung UniversityTaoyuan
  2. 2.Department of SurgeryVeteran General HospitalTaoyuan
  3. 3.Institute of Life ScienceNational Tsing Hwa UniversityHsinchuTaiwan

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