Characterization of the estrogen receptor extracted from hen oviduct nuclei with pyridoxal phosphate.
The estrogen receptor was extracted in high yield from nuclei of laying hen oviduct with 10 mM pyridoxal-5'-phosphate (PLP). The receptor extracted under these conditions, unlike that extracted with 0.4 M KCl, displayed no tendency to aggregate on sucrose gradients in low salt. The receptor was eluted as a single peak from DEAE-Sephacel at an ionic strength of 0.13 M KCl. The receptor after DEAE chromatography had approximately half the molecular weight of that in the nuclear extract. A larger form could be reconstituted by the addition of whole nuclear extract to the DEAE eluate. These data support the notion that the nuclear estrogen receptor is a dimer composed of similar subunits.
D000818:Animals; D002467:Cell Nucleus / Q000032:analysis; D002499:Centrifugation, Density Gradient; D002645:Chickens; D002852:Chromatography, Ion Exchange; D005260:Female; D010057:Oviducts / Q000032:analysis*; D011732:Pyridoxal Phosphate / Q000494:pharmacology*; D011960:Receptors, Estrogen / Q000302:isolation & purification*
D011960:Receptors, Estrogen; D011732:Pyridoxal Phosphate