Increased binding to DNA-cellulose of the unactivated and activated glucocorticoid-receptor complex from mouse brain following sucrose density gradient ultracentrifugation.

The binding to DNA-cellulose of both the unactivated and activated forms of the molybdate-stabilized glucocorticoid-receptor complex increases markedly after subjecting these preparations to sucrose density gradient ultracentrifugation. We speculate that this increase results from the removal of endogenous macromolecular factors which competitively inhibit glucocorticoid receptor binding to DNA and which may normally be involved in regulating the genomic responses of these steroids in brain.