[Various properties of partially purified dexamethasone receptor complexes of the rat liver]

A 300-fold purification of glucocorticosteroid-receptor complexes (GRC) of the rat liver with the 10--25% yield was conducted by combining the methods of binding with DNA-cellulose and salting out with ammonium sulfate at 30% saturation. An important feature of this method was a preponderant removal of protein admixtures capable of dissociation with DNA. In comparison of column chromatography and batch-procedure the latter proved to possess a number of advantages. Some properties of partially purified GRC were also studied. As revealed, the purified GRC which rapidly decomposed at 2 degrees C, could be partially stabilized by addition of inert protein, glycerine, SH-reagents and an excess of dexamethazone. Under such conditions about 13% of the initial amount of purified GRC was preserved after a week of storage at 2 degrees C. Determination of purified GRC content in the preparation by sorption on dextran coated carbon gave sharply diminished results; as to the method of oxyapatite sorption--it proved to be adequate. In comparing the GRC properties without and after the purification demonstrated that sedimentation and other properties of these preparations largely coincided. GRC-acceptor capacity of one- and two-chain DNA depended to a different degree on cytoplasmic admixtures in the GRC preparation removed in its purification.