An antiserum to the rat liver glucocorticoid receptor.
A rabbit immunized with a highly purified preparation of rat liver [3H]triamcinolone-receptor complex developed antibodies to the receptor. Although precipitating reactions were not detected, complexes formed between IgG and the receptor could be detected by Staphylococcus aureus protein A-Sepharose and gel permeation chromatography. IgG was purified and covalently immobilized on Sepharose CL-4B; this affinity matrix adsorbed the ligand-free receptor and both activated and nonactivated forms of the [3H]triamcinolone-receptor complex. Rat liver cytosol proteins adsorbed by control and immune immunoglobulin-Sepharoses were eluted with 0.1 M acetic acid and analyzed by sodium dodecyl sulfate/polyacrylamide gel electrophoresis. A protein with molecular weight 78,000 was the major species eluted from immune immunglobulin-Sepharose, and it was not present in eluates from control columns. Rat transcortin, glucocorticoid binder IB, and an estrogen-binding protein from rat liver were not adsorbed by immune IgG-Sepharose. Mouse and hamster liver glucocorticoid receptors showed only limited adsorption. Thus, the antiserum does not crossreact with other major glucocorticoid-binding proteins and demonstrates species specificity.
D000818:Animals; D000906:Antibodies / Q000302:isolation & purification*; D000918:Antibody Specificity; D006224:Cricetinae; D003429:Cross Reactions; D005260:Female; D007163:Immunosorbent Techniques; D008297:Male; D008647:Mesocricetus; D051379:Mice; D051381:Rats; D011965:Receptors, Glucocorticoid / Q000276:immunology* / Q000378:metabolism; D011987:Receptors, Steroid / Q000276:immunology*; D013045:Species Specificity; D014221:Triamcinolone / Q000378:metabolism
D000906:Antibodies; D011965:Receptors, Glucocorticoid; D011987:Receptors, Steroid; D014221:Triamcinolone