PMID: 3736036Jun 1, 1986Paper

Biochemical characterization of the progesterone receptor in the chick bursa of Fabricius

Journal of Steroid Biochemistry
T Ylikomi


In a previous work we demonstrated estrogen-inducible progesterone binding sites in the bursa of Fabricius. In the present study these were characterized and compared to the progesterone receptor (PR) in the chick oviduct. When the size of the binding sites was analyzed with sucrose gradient centrifugation, 2 peaks of bound progesterone were obtained. The sedimentation coefficients of the peaks were 8-9 S and 3-4 S. In size exclusion HPLC only 1 peak was seen with a size corresponding to the 8-9 S in the sucrose gradient. The Stokes radius was 7.7 nm. When the ionic strength was elevated or CaCl2 was added, smaller steroid binding forms were detected. The sizes of these progesterone binding molecules at low and high ionic strength and in the presence of CaCl2 were equal in bursa and oviduct when analyzed with HPLC. The Stokes radii of these forms were 5.6 nm in high salt and 2.1 nm with CaCl2. The steroid binding components in the bursa cytosol eluated as 2 peaks from the DEAE column with KCl gradient. The peaks corresponded to the so-called A and B components in the chick oviduct. In the presence of molybdate, bound progesterone eluated as one peak from DEAE in both oviduct and bursa. The progesterone binding capacity was show...Continue Reading


Sep 1, 1979·Journal of Steroid Biochemistry·C J GrossmanP Nathan
May 12, 1972·Biochemical and Biophysical Research Communications·K KontulaR Vihko
Aug 1, 1984·Molecular and Cellular Endocrinology·J M Renoir, J Mester
Oct 1, 1983·Endocrinology·P T PearceJ W Funder
Mar 15, 1980·Developmental Biology·N M Le DouarinE E Baulieu
Nov 1, 1980·General and Comparative Endocrinology·E A PederneraM C Aguilar

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Jan 1, 1988·Journal of Steroid Biochemistry·T Ylikomi, P Tuohimaa
Jul 1, 1987·Molecular and Cellular Endocrinology·T J YlikomiP J Tuohimaa

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