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• W2080494503 abstract "Dexamethasone (DXM) was found to bind with high affinity to a macromolecular component of the bovine adrenal cortex cytosol. Using an equilibrium dialysis technique, an apparent dissociation constant Kd of about 10−7m and a binding capacity of 6 pmol/mg of protein were obtained for DXM. A lower binding ability was exhibited by the natural glucocorticosteroids, whereas aldosterone, androgens, and oestrogens were not competitors. The association and dissociation processes were completed in less than 5 min. The DXM binder sedimented as a 7 S moiety upon density gradient centrifugation at low or high ionic strength, and chromatographed on Sephadex G-200 as a macromolecule of about 150,000 molecular weight. The binding was destroyed by treatment with trypsin and Pronase and inhibited by N-ethylmaleimide, but was not affected by DNase or RNase. Upon incubation with cytosol in vitro at 37 °C, the metabolism of DXM was limited, whereas cortisol was extensively transformed. No significant metabolism was detected for either compound upon incubation at 0 °C. Although this high affinity binding may be related to some of the known effects of corticosteroids on the adrenal cell, it did not possess several of the usual characteristics of target tissue steroid receptor. Therefore, its biological significance must await further investigation to be understood." @default.
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• W2080494503 date "1977-04-01" @default.
• W2080494503 modified "2023-10-04" @default.
• W2080494503 title "A soluble glucocorticoid binding protein in the bovine adrenal cortex" @default.
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• W2080494503 doi "https://doi.org/10.1016/0003-9861(77)90001-7" @default.
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