Tight binding of glucocorticoid-receptor complexes to histone-agarose |
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Authors: | K Ueda F Isohashi K Okamoto I Kokuhu K Kimura K Yoshikawa Y Sakamoto |
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Institution: | Department of Dermatology, Osaka University Medical School, Japan. |
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Abstract: | "Activated" glucocorticoid-receptor complexes purified about 3,000-fold from rat liver were found to bind to histone-agarose. Because of their tight binding, they could not be eluted from the column by high salt solution (3 M KCl) or low salt plus polyol buffer (50% ethylene glycol), but their binding could be disrupted by pyridoxal 5'-phosphate; more than 70% recovery of the "activated" receptor complexes was achieved with buffer containing 20 mM pyridoxal 5'-phosphate. This interaction of "activated" glucocorticoid-receptor complexes of rat liver with histone-agarose suggests a role of histones in the mechanism of action of steroid hormone. |
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