Rat liver glucocorticoid-receptor complexes (GRC) acquire the ability to bind to DNA in a high affinity manner after activation by heating or precipitation with (NH)2SO4. DNA is practically non-saturable by GRC in low salt buffers as well as in 0.15 M NaCl-containing buffer, although in the latter case the binding decreases approximately 3--5 times. GRC bind to homo- and heterologous prokaryotic DNA in a similar way; in both cases an addition of KCl (up to 0.15 M) to the medium is followed by the same decrease of the binding. This data suggest that the association of GRC with DNA observed in vitro is not accompanied by "recognition" of any certain DNA site. Besides DNA, activated GRC can associate with other polymers, charged positively (DEAE-cellulose) or negatively (RNA, polyvinylsulfate). GRC interact very weakly with neutral compounds of the cellulose type but are strongly adsorbed on hydroxyapatite. Hence the activated GRC can be considered as an amphoteric protein. Salt solutions provoke dissociation of the GRC-DNA triple complexes: a complete dissociation is observed in the presence of 0,4 M NaCl or 0,4 M sodium phosphate buffer (pH 6,9). Sodium phosphate buffer also elutes GRC from other sorbents such as DEAE-cellulose or hydroxyapatite. No significant dissociation of the GRC-DNA complexes is observed at sucrose concentration up to 2 M. The data obtained are indicative of an essential role of electrostatic forces for the interaction of GRC with DNA. The non-ionic detergent Triton X-100 at a concentration as low as 0,05% completely destroys the GRC-DNA triple complexes. The models explicating the selectivity of the genome activation by GRC without their "recognition" of any specific DNA sequences are proposed.