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- W2530001612 abstract "The possible interaction of progesterone- receptor complexes with nucleotides was tested by affinity chromatography. The cytosol progesterone receptor from hen oviduct was partially purified by ammonium sulfate precipitation before use. When progesterone was bound to the receptor, the resulting complex could be selectively adsorbed onto columns of ATP-Sepharose. This inter- action was reversible and of an ionic nature since it could be disrupted by high-salt conditions. A competitive bind- ing assay was used to test the specificity of receptor bind- ing to several other nucleotides, including ADP, AMP, and cAMP. A clear specificity for binding ATP was evident from these studies. When ATP was added to receptor preparations, the nucleotide did not affect the sedimenta- tion properties or hormone binding characteristics of the receptor. Although the function' of ATP remains un- known, these studies indicate a role of this nucleotide in some aspect of hormone receptor activity. An initial step in the mechanism of steroid hormone action involves binding of the steroid to receptor proteins in the target cell. The resulting complex then migrates into the" @default.
- W2530001612 created "2016-10-21" @default.
- W2530001612 creator A5077259729 @default.
- W2530001612 date "2016-01-01" @default.
- W2530001612 modified "2023-09-27" @default.
- W2530001612 title "Binding of ATP to the Progesterone Rece (hen oviduct/affinity chromatography/ATP-Sepharose)" @default.
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- W2530001612 hasPublicationYear "2016" @default.
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