Activation of the rat liver glucocorticoid-receptor complex

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Abstract
The rat liver glucocorticoid receptor was activated using 3 procedures: heat, gel filtration and dilution. With time after heat activation the steroid-receptor complex loses its capacity to bind to DNA-cellulose, while receptor activated by Sephadex G-25 and by dilution maintains DNA-cellulose binding capacity. The rates of steroid dissociation from nonactivated and activated receptor are essentially identical. Nonactivated receptor is capable of rebinding steroid, while activated receptor has a reduced capacity to rebind steroid. The results of the gel filtration and dilution studies suggest that a low-molecular-weight factor(s) exists in rat liver cytosol which is involved in the process of activation.