Abstract
Steroid hormones produce a response in target cells by binding to hormone-specific soluble receptors, which undergo a transformational change, leading to their interaction with chromatin and to modified gene expression. In a previous paper1, we described a monoclonal antibody, BF4, that specifically recognizes and binds the non-transformed ‘8S’ form of chicken oviduct progesterone receptor (8S–PR). We now show that BF4 does not form an immune complex with the 4S transformed form of 3H-progestin-labelled progesterone receptor, but does interact with the 8S non-transformed forms of the oestrogen, androgen and glucocorticosteroid receptors. Our results suggest that the antigenic determinant recognized by BF4 is present on a non-hormone binding unit, which we identify as a polypeptide of molecular weight (MW) 90,000 in the case of the progesterone receptor, and that this unit is common to other 8S non-transformed chicken steroid receptors.
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Joab, I., Radanyi, C., Renoir, M. et al. Common non-hormone binding component in non-transformed chick oviduct receptors of four steroid hormones. Nature 308, 850–853 (1984). https://doi.org/10.1038/308850a0
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DOI: https://doi.org/10.1038/308850a0
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