M. Dautrevaux

TL;DR: Rat liver glucocorticoid receptor was purified in the presence of molybdate by a three-step procedure comprising protamine sulfate precipitation, affinity chromatography on a dexamethasone matrix and high-performance size-exclusion chromatography (HPSEC) on a TSK G 3000 SW column, which yielded an almost homogeneous 90 000-Mr band.

TL;DR: The data, demonstrating for the first time that all antiglucocorticoids probably act via a common mechanism, suggest a key role for subunit dissociation during in vivo receptor activation.

TL;DR: The synthesis of biospecific adsorbents for the purification of the cytosol glucocorticoid receptor from rat liver is described, selecting a dexamethasone derivatized agarose on the basis of its stability, its binding specificity and reversibility.

TL;DR: The cytosolic untransformed molybdate-stabilized glucocorticoid-receptor complex from rat liver was eluted as a heterogenous peak containing two components with Stokes radii, demonstrating that the 7.1-nm component could not result from a proteolytic degradation of the 8.3-nm receptor form and suggesting that an endogenous RNase is not involved in the transformation process.

TL;DR: Two antihormones which have different structures show the same behavior towards the glucocorticoid-receptor complex by strikingly reducing both the activation process and the size reduction of the steroid-re receptor complex which is concomitant to activation and which could constitute the first step of this process.