The association of glucocorticoid-receptor complexes with other components in vivo has been evaluated by chemical crosslinking of hormone-treated cells. When cells were incubated with hormone at 2 degrees C, before being subjected to crosslinking, most glucocorticoid-receptor complexes were found untransformed, as judged by DEAE-cellulose chromatography, and sedimented as 11-6 S oligomers in sucrose gradients containing 0.3 M NaCl. If crosslinking was performed after cells were treated with hormone at 37 degrees C, about 60% of cytosolic glucocorticoid-receptor complexes were found transformed, and sedimented as 4 S monomers.
TRANSFORMATION OF GLUCOCORTICOID-RECEPTOR COMPLEXES IS ACCOMPANIED BY DISSOCIATION OF OLIGOMERS IN INTACT-CELLS / Rossini, Gian Paolo; Malaguti, C.. - In: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS. - ISSN 0006-291X. - STAMPA. - 170:(1990), pp. 1210-1215.
TRANSFORMATION OF GLUCOCORTICOID-RECEPTOR COMPLEXES IS ACCOMPANIED BY DISSOCIATION OF OLIGOMERS IN INTACT-CELLS
ROSSINI, Gian Paolo;
1990
Abstract
The association of glucocorticoid-receptor complexes with other components in vivo has been evaluated by chemical crosslinking of hormone-treated cells. When cells were incubated with hormone at 2 degrees C, before being subjected to crosslinking, most glucocorticoid-receptor complexes were found untransformed, as judged by DEAE-cellulose chromatography, and sedimented as 11-6 S oligomers in sucrose gradients containing 0.3 M NaCl. If crosslinking was performed after cells were treated with hormone at 37 degrees C, about 60% of cytosolic glucocorticoid-receptor complexes were found transformed, and sedimented as 4 S monomers.
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