In odder to provide a further insight into glucocorticoid receptor (GR)-mediated action of glucocorticoid hormones, we produced ten monoclonal antibodies against rat GR. In studies combining physicochemical separation methods with antibody methodology, we established that the molybdate-stabilised GR contains one steroid-binding monomer. Using a monoclonal anti-GR antibody-based immunoaffinity chromatographic procedure, we purified two non-ligand-binding proteins, with molecular weights of 80,000 and 90,000, present in the molybdate-stabilised GR complex. These proteins are not recognised by monoclonal antibodies directed against GR. The possible relation of these two proteins to heat shock proteins remains to be established.
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