Kinetic analyses of activation-induced changes in the hydrodynamic and surface properties of the glucocorticoid-receptor complex in mouse brain.

Unactivated, molybdate-stabilized, [3H]triamcinolone acetonide-labeled, glucocorticoid receptors from mouse whole brain were activated by removal of the molybdate and incubation at 22 degrees C for 1.5 to 24 min and then rapidly quenched at 0 degrees C with molybdate. The loss of the 9.2 S (unactivated) form of the [3H]TA-receptor complex and the concomitant formation of the 3.8 S (activated) form displayed first-order kinetics with a half-time of less than two min. The increase in the 3.8 S form correlated nearly perfectly with an increased binding to DNA-cellulose, and with a decreased and increased adsorption to DEAE-cellulose and glass fiber filters, respectively. The changes in adsorption to these filters, which occurred at a faster rate than did the changes in binding to DNA-C, are thought to reflect an increase in the relative number of positive charges and hydrophobic groups on the surface of the activated complex.