Conservation of the DNA binding domain and other properties between porcine and rat glucocorticoid receptors.
作者： Andrew R. Marks , David D. Moore , Douglas I. Buckley , Bahiru Gametchu , Howard M. Goodman
DOI: 10.1016/0022-4731(86)90369-9
关键词:
摘要: 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 protocol developed for purification rat GCR [1–2]. This preparation, when separated SDS-polyacrylamide gel electrophoresis immunoblotted, indicated that Mr = 94,000 band cross-reacts with monoclonal antibody against [3]. A nitrocellulose filter binding assay showed both the GCRs interact specifically cloned synthetic 24 base pair deoxyoligonucleotide containing sequence in first intron human growth hormone (hGH) gene [4]. specific protein-DNA interaction is blocked single change site. All three putative domains molecule: steroid binding, immunoreactive, DNA have been conserved between two divergent species.
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