Identification of two forms of progesterone receptor from chick oviduct cytosol using non-denaturing gel electrophoresis.
Non-denaturing polyacrylamide gel electrophoresis and non-denaturing agarose gel electrophoresis have been used to resolve [3H]R5020-binding components from chick oviduct cytosol. From both gel systems 2 peaks of bound radioactivity are resolved which display these properties of authentic progesterone receptor: binding of R5020: steroid specificity, saturability, and restriction to target tissues. The two peaks are approximately equal in magnitude, and there is no evidence for interconversion of the 2 peaks. The presence or absence of 10-20 mM sodium molybdate during cytosol preparation had no effect on the magnitude or mobility of either peak. Neither peak contains salt-dissociable components which affect its electrophoretic properties, suggesting a possible alteration of native receptor forms during electrophoresis.
Smith
D F
DF
Skipper
J K
JK
Davidson
F I
FI
Hamilton
T H
TH
D000818:Animals; D002645:Chickens; D003600:Cytosol / Q000378:metabolism; D004054:Diethylstilbestrol / Q000494:pharmacology; D004587:Electrophoresis, Agar Gel / Q000379:methods; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D005260:Female; D010057:Oviducts / Q000187:drug effects / Q000378:metabolism*; D011397:Promegestone / Q000378:metabolism; D011489:Protein Denaturation; D011980:Receptors, Progesterone / Q000187:drug effects / Q000302:isolation & purification / Q000378:metabolism*
D011980:Receptors, Progesterone; D004054:Diethylstilbestrol; D011397:Promegestone