Purification of a full-length recombinant glucocorticoid receptor.
We described a novel purification method for a recombinant glucocorticoid receptor (GR) in detail. The purification procedure consists of sequential chromatographies using common ion-exchange columns (Mono Q and Mono S). This procedure is based upon a new finding that the activated GR binds both to a Mono Q column and to a Mono S column at the same pH. The entire chromatographies took about 3 h and GR represented 97% of the purified protein sample. This purification protocol will be applicable to the purification of native GR, point-mutated recombinant GR and other nuclear receptors.
Okamoto
Kazuki
K
Department of Biochemistry, St. Marianna University School of Medicine, 2-16-1 Sugao, Miyamae-ku, Kawasaki, 216-8511, Kanagawa, Japan.
Suematsu
Naoya
N
Isohashi
Fumihide
F
D002852:Chromatography, Ion Exchange / Q000379:methods; D004591:Electrophoresis, Polyacrylamide Gel; D011965:Receptors, Glucocorticoid / Q000302:isolation & purification*; D011994:Recombinant Proteins / Q000302:isolation & purification
D011965:Receptors, Glucocorticoid; D011994:Recombinant Proteins