title: Conservation of the DNA binding domain and other properties between porcine and rat glucocorticoid receptors.
abstract: Activated glucocorticoid receptor protein (GCR) was partially purified from porcine liver cytosol by sequential chromatography on phosphocellulose and DNA-cellulose using a modification of a protocol developed for purification of rat GCR. This partially purified preparation, when separated by SDS-polyacrylamide gel electrophoresis and immunoblotted, indicated that a Mr = 94,000 protein band cross-reacts with a monoclonal antibody against rat GCR. A nitrocellulose filter binding assay showed that both the partially purified porcine and rat GCRs interact specifically with a cloned synthetic 24 base pair deoxyoligonucleotide containing the GCR binding sequence in the first intron of the human growth hormone (hGH) gene. This specific protein-DNA interaction is blocked by a single base pair change in the binding site. All three putative domains of the GCR molecule: the steroid binding, immunoreactive, and DNA binding have been conserved between two divergent species.
mesh_terms: D000818:Animals; D000911:Antibodies, Monoclonal; D001483:Base Sequence; D002846:Chromatography, Affinity; D003101:Collodion; D004591:Electrophoresis, Polyacrylamide Gel; D007158:Immunologic Techniques; D008297:Male; D009154:Mutation; D051381:Rats; D011956:Receptors, Cell Surface / Q000235:genetics / Q000302:isolation & purification*; D011965:Receptors, Glucocorticoid / Q000235:genetics / Q000302:isolation & purification*; D011986:Receptors, Somatotropin; D013045:Species Specificity; D013552:Swine
chemical_list: D000911:Antibodies, Monoclonal; C033365:DNA receptor; D011956:Receptors, Cell Surface; D011965:Receptors, Glucocorticoid; D011986:Receptors, Somatotropin; D003101:Collodion