Abstract
DNA-cellulose chromatography was used to purify the glucocorticoid receptor from rat liver. The heat-activated [ 3H]-dexamethasone-receptor complex bound to DNA-cellulose in the presence of 0.1 M NaCl and could be eluted with 0.45 M NaCl. [ 3H]-Dexamethasone-receptor complex that had not been heat-activated did not bind to DNA-cellulose. Using a single column of DNA-cellulose the receptor could be purified 40-fold. The partially purified [ 3H]-dexamethasone-receptor complex was able to bind to isolated liver nuclei.
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