• Title of article

    New purification method for glucocorticoid receptors

  • Author/Authors

    Okamoto، نويسنده , , Kazuki and Isohashi، نويسنده , , Fumihide، نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 2003
  • Pages
    5
  • From page
    367
  • To page
    371
  • Abstract
    In this report, we describe a new purification method for activated recombinant glucocorticoid receptor (GR) utilizing a cation-exchanger (Mono S) at pH 8.4. 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.
  • Keywords
    reviews , Glucocorticoid receptor , Purification
  • Journal title
    Journal of Chromatography B
  • Serial Year
    2003
  • Journal title
    Journal of Chromatography B
  • Record number

    1456118