title: New purification method for glucocorticoid receptors.
abstract: In this report, we describe a new purification method for activated recombinant glucocorticoid receptor (GR) utilizing a cation-exchanger (Mono S) at pH8.4. This method is based upon a new finding that activated GR binds to both Mono Q and Mono S columns at the same pH. This method enables us to purify recombinant GR within 3 h. The purified GR represents more than 97% of the eluted proteins. Purified recombinant GR is able to bind specifically to a DNA fragment containing the glucocorticoid response element. Recombinant GR has no tag sequence that can be utilized for purification. Thus, this separation method is also applicable to purification of native GR.
authors: Department of Biochemistry, St. Marianna University School of Medicine, 16-1 Sugao 2 chome, Miyamae, Kawasaki, Kanagawa 216-8511, Japan.
authors: Kazuki
authors: K
authors: Okamoto
authors: Fumihide
authors: F
authors: Isohashi
mesh_terms: D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D051381:Rats; D011965:Receptors, Glucocorticoid / Q000302:isolation & purification*; D011994:Recombinant Proteins / Q000302:isolation & purification; D018411:Spodoptera
chemical_list: D011965:Receptors, Glucocorticoid; D011994:Recombinant Proteins