Partial purification of the activated hepatic glucocorticoid - receptor complex.

A rapid procedure for the purification of the hepatic glucocorticoid receptor has been developed which exploits the observation that "activation" of this complex enables it to bind to anionic substances such as DNA and phosphocellulose. The procedure consists of two phosphocellulose columns operated in sequence. The first column removes from unfractionated cytosol all basic proteins which adhere to the immobilized phosphate residues; the steroid - receptor complex elutes in the flow-through of this first column. This complex is then thermally activated and applied to a second phosphocellulose column where it is retained, washed, and eluted by a salt gradient. This simple procedure is capable of purifying the steroid - receptor complex over 1000-fold.