Progesterone binding to hen oviduct genome: specific versus nonspecific binding.
Data are presented to explain discrepancies in the literature involving the in vitro binding of steroid receptor complexes to isolated nuclei and chromatin. The type of binding in vitro of the progesterone-receptor complex to nuclei, chromatin, or DNA of hen organs is largely determined by the ionic strength of the medium. Low ionic conditions (0.01 to 0.05 molar potassium chloride) result in a nonspecific, nonsaturable binding, while high ionic conditions (0.15 to 0.20 molar potassium chloride) create a tissue-specific, saturable binding. Pure DNA binds the steroid receptor complex extensively in low salt but very little in the higher salt conditions.
D000818:Animals; D002467:Cell Nucleus / Q000378:metabolism; D002645:Chickens; D002843:Chromatin / Q000378:metabolism; D004247:DNA / Q000378:metabolism; D005260:Female; D009994:Osmolar Concentration; D010057:Oviducts / Q000378:metabolism*; D011374:Progesterone / Q000378:metabolism*; D011956:Receptors, Cell Surface; D013154:Spleen / Q000378:metabolism
D002843:Chromatin; D011956:Receptors, Cell Surface; D011374:Progesterone; D004247:DNA