[Hydrocortisone-receptor complex binding with various nonhistone protein groups].
Complexes containing DNA and various groups of non-histone proteins were isolated from rat liver cells. Deproteinized DNA was bound with the hydrocortisone-receptor complex at the highest rate in vitro. Non-histone proteins from the chromatin fraction did not bind with the hormone-receptor complex. Unsaturability of DNA in reaction with the complex appears to indicate the low specificity of binding.
D000818:Animals; D002843:Chromatin / Q000378:metabolism; D002868:Chromosomal Proteins, Non-Histone / Q000378:metabolism*; D003600:Cytosol / Q000378:metabolism; D004247:DNA / Q000378:metabolism; D005260:Female; D006854:Hydrocortisone / Q000378:metabolism*; D066298:In Vitro Techniques; D008099:Liver / Q000378:metabolism; D008297:Male; D011485:Protein Binding; D051381:Rats; D011965:Receptors, Glucocorticoid / Q000378:metabolism*; D011987:Receptors, Steroid / Q000378:metabolism*
D002843:Chromatin; D002868:Chromosomal Proteins, Non-Histone; D011965:Receptors, Glucocorticoid; D011987:Receptors, Steroid; C029360:hydrocortisone receptor; D004247:DNA; D006854:Hydrocortisone
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