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  • Title: Evidence for two structurally related progesterone receptors in chick oviduct cytosol.
    Author: Gronemeyer H, Harry P, Chambon P.
    Journal: FEBS Lett; 1983 Jun 13; 156(2):287-92. PubMed ID: 6852262.
    Abstract:
    The existence of two progesterone receptor forms present in crude cytosol of chick oviduct has been demonstrated by photoaffinity labelling using [3H]R5020. On SDS-polyacrylamide gels these two forms exhibit app. Mr-values of 79000 and 109000 corresponding to the progesterone receptor forms A and B. Peptide maps of photoaffinity-labelled steroid receptors have been established by limited proteolysis with alpha-chymotrypsin. The peptide map obtained for chick oviduct cytosol progesterone receptor crosslinked with [3H]R5020 proved to be the sum of peptides obtained from partially purified preparations of forms A and B. The peptide maps of both progesterone receptor forms were identical for peptides below the Mr-value of form A, indicating extensive homology of the two forms. A significantly different peptide pattern was observed for the rat liver glucocorticoid receptor crosslinked with [3H]triamcinolone acetonide. Prolonged proteolysis with chymotrypsin gave rise to peptides with Mr-values of 6000 and 10000 from the hormone-binding domain of progesterone and glucocorticoid receptors, respectively.
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