Characterization of glucocorticoid receptors in S49 mouse lymphoma cells by affinity labeling with [3H]dexamethasone 21-mesylate
作者： Clark W. Distelhorst , Laurie Kullman , Jon Wasson
DOI: 10.1016/0022-4731(87)90031-8
关键词: Gel electrophoresis 、 Chymotrypsin 、 Glucocorticoid receptor 、 Mutant 、 Molecular biology 、 Cytosol 、 Wild type 、 Affinity labeling 、 Receptor 、 Biology
摘要: Abstract Glucocorticoid receptors in wild type and mutant S49 mouse lymphoma cells were affinity labeled with [ 3 H]dexamethasone 21-mesylate analyzed directly by sodium dodecyl sulfatepolyacrylamide gel electrophoresis. The molecular weight of cytosol from nuclear transfer decreased (nt − ) mutants was 97,000 (97kDa). increased i 48 kDa. 97 kDa receptor digested chymotrypsin to a 40 steroid-binding fragment but the nf resistant digestion chymotrypsin. In addition receptor, nt contained 18 fragments. Cytosol also fragments present multiple subclones cell line. Formation these not prevented protease inhibitors extended incubation samples. Both forms form, could be activated bound DNA-cellulose.
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