The avian progesterone receptor: isolation and characterization of phosphorylated forms.
Methods have been developed for isolation of the avian progesterone receptor in the nontransformed, molybdate-stabilized state. The final step in this procedure. DEAE-Sephadex chromatography, resolves the receptor into two forms, components I and II. Analysis of these components by polyacrylamide gel electrophoresis under denaturing conditions shows that both contain a peptide with Mr = 90,000. These peptides contain phosphorylated serine residues, as shown by [32P]orthophosphate incorporation studies. When the cytosol receptor is treated with alkaline phosphatase, its steroid binding capacity is abolished. These studies show that the nontransformed progesterone receptor is a phosphoprotein and indicate that receptor phosphorylation may be important to the maintenance of steroid binding capacity.
D000469:Alkaline Phosphatase / Q000378:metabolism; D000818:Animals; D002645:Chickens; D002847:Chromatography, Agarose; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D008970:Molecular Weight; D010057:Oviducts / Q000032:analysis; D010766:Phosphorylation; D011980:Receptors, Progesterone / Q000302:isolation & purification*
D011980:Receptors, Progesterone; D000469:Alkaline Phosphatase