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Progesterone Receptors of Chick Oviduct

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Hormone Receptors

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 96))

Abstract

The chick oviduct progesterone receptor has been purified to homogeneity by affinity chromatography and its molecular action studied in vitro. The native receptor is a 200,000 MW dimer of two dissimilar 4S subunits with different intranuclear function. The receptors directly regulate RNA chain initiation sites in oviduct chromatin by interactions involving target tissue nuclear acceptor sites. There is a 1:1 correspondence between receptor “acceptor” sites and RNA sites. Only the dimer form of the receptor is active in vitro on chromatin templates. The study suggests a novel model for hormone action which can be tested directly in this system.

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Authors and Affiliations

  1. Department of Cell Biology, Baylor College of Medicine, Houston, TX, 77030, USA

    William T. Schrader & Bert W. O’Malley

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  1. William T. Schrader
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  2. Bert W. O’Malley
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Editors and Affiliations

  1. University of Missouri-Columbia, USA

    David M. Klachko M.D. (Associate Professor of Medicine), Leonard R. Forte Ph.D. (Associate Professor of Pharmacology) & John M. Franz Ph.D. (Associate Professor of Biochemistry) (Associate Professor of Medicine),  (Associate Professor of Pharmacology) &  (Associate Professor of Biochemistry)

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Schrader, W.T., O’Malley, B.W. (1978). Progesterone Receptors of Chick Oviduct. In: Klachko, D.M., Forte, L.R., Franz, J.M. (eds) Hormone Receptors. Advances in Experimental Medicine and Biology, vol 96. Springer, New York, NY. https://doi.org/10.1007/978-1-4757-0722-9_4

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  • DOI: https://doi.org/10.1007/978-1-4757-0722-9_4

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