Abstract
WHEN 17β-oestradiol and other oestrogens enter a target cell they are bound by highly specific oestrophilic proteins in a strong but non-covalent manner (Kass≃1.3 × 109–1.5 × 109 M−1 for 17β-oestradiol)1. These oestrogen receptors are found in both nuclear and cytoplasmic fractions of uterus and other target organs to this hormone1–11. We now report (1) that iodination of calf uterus oestrogen receptors in alkaline media at lowered temperature destroys their ability to bind 17β-oestradiol; (2) that this effect cannot be ascribed to oxidation of SH groups; and (3) that iodination is ineffective when the binding site is interacting with the hormone, and is thus protected from a direct effect.
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PUCA, G., BRESCIANI, F. Binding Activity of Oestrogen Receptors destroyed by Iodination. Nature 225, 1251–1252 (1970). https://doi.org/10.1038/2251251a0
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DOI: https://doi.org/10.1038/2251251a0
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