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Tight binding of glucocorticoid-receptor complexes to histone-agarose.

作者信息

Ueda K, Isohashi F, Okamoto K, Kokuhu I, Kimura K, Yoshikawa K, Sakamoto Y

机构信息

Department of Dermatology, Osaka University Medical School, Japan.

出版信息

Biochem Biophys Res Commun. 1988 Mar 15;151(2):763-7. doi: 10.1016/s0006-291x(88)80346-2.

DOI:10.1016/s0006-291x(88)80346-2
PMID:3348810
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.

摘要

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