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  • Title: Structural relationships between the chick oviduct progesterone receptor A and B proteins.
    Author: Vedeckis WV, Schrader WT, O'Malley BW.
    Journal: Adv Exp Med Biol; 1979; 117():309-27. PubMed ID: 474284.
    Abstract:
    The chick oviduct contains two distinct forms of the progesterone receptor, termed progestophilins A (Mr = 79,000) and B (Mr = 117,000). Although these two hormone-binding proteins differ significantly in physico-chemical characteristics, a good deal of similarity exists between these two molecules. Thus, both proteins display identical hormone-binding kinetics and steroid specificity. The hormone-binding fragments obtained after the action of an endogenous oviduct Ca2+-activated protease are indistinguishable as analyzed by gel filtration chromatography. Both the A and B proteins are capable of binding to DNA-cellulose, although they elute at very different salt concentrations when subjected to gradient elution. In spite of these similarities all attempts to demonstrate the conversion of progestophilin B to A or to show a common precursor to both have been unsuccessful. Therefore, either the A and B receptor proteins are separate products of closely related genes or the conversion of one form to another occurs very rapidly either in vivo or in vitro.
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