Origin and Quantification of Cytoplasmic Estradiol Receptor in Resting Target Cells
- 1 January 1983
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 364 (2) , 1497-1506
- https://doi.org/10.1515/bchm2.1983.364.2.1497
Abstract
The exhaustive extraction of microsomal estradiol receptor by surfynol/dithiothreitol/trypsin in low ionic strength buffer was employed for distribution studies on non-stimulated porcine endometrium. More than 1/2 of the cytoplasmic receptor contents were of microsomal orgin. Empty structures did not interfere with receptor analysis by agar-gel electrophoresis. The combined yields from homogenate-fractions corresponded to those obtained from unfractionated homogenates. Freeze-fracturing of endometrium had a moderate receptor-solubilizing effect.This publication has 6 references indexed in Scilit:
- Structural Assignment and Extractability of Microsomal Estradiol ReceptorsHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1983
- Characterization of Microsomal Subfractions from Porcine Endometrium CellsHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1983
- The Occurrence of Steroid-Free, “Activated” Estrogen Receptor in Target Cell NucleiHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1978
- Cytoplasmic Estradiol “Receptors” Associated with the “Microsomal” Fraction of Pig UterusHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1972
- Characterization and Assay of Steroid Hormone Receptors and Steroid-Binding Serum Proteins by Agargel Electrophoresis at Low TemperatureHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1972