Colman P D, Feigelson P
Mol Cell Endocrinol. 1976 Jun-Jul;5(1-2):33-40. doi: 10.1016/0303-7207(76)90068-x.
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.
已开发出一种快速纯化肝糖皮质激素受体的方法，该方法利用了这样一个观察结果：这种复合物的“激活”使其能够与阴离子物质如DNA和磷酸纤维素结合。该方法由两个依次操作的磷酸纤维素柱组成。第一根柱子从未分级的细胞溶质中去除所有附着在固定化磷酸残基上的碱性蛋白质；类固醇-受体复合物在第一根柱子的流出物中洗脱。然后将该复合物进行热激活，并应用于第二根磷酸纤维素柱，在那里它被保留、洗涤并通过盐梯度洗脱。这个简单的方法能够将类固醇-受体复合物纯化1000倍以上。
