Abstract

Glucocorticoid-receptor complexes in rat thymus cytosol were characterized by gel-filtration chromatography on Agarose A-1.5 m and Sephacryl S-300. Two forms of non-transformed complex were identified at low ionic strength in the presence of molybdate, with Stokes radii of approx 8 nm and 6 nm. The 8 nm molybdate-stabilized form could be converted to the 6 nm form by chromatography on Sephacryl S-300 or Lipidex 1000 or by incubation with dextran-charcoal or phospholipase C, but not by chromatography on Sephadex G-25; none of the treatments promoted receptor transformation. It is suggested that the change in Stokes radius from 8 to 6 nm results from the removal of a lipid factor responsible for maintaining the complex in the 8 nm form.

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