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Prolactin Receptors

Purification, Molecular Weight, and Binding Specificity

  • Chapter
Receptor Purification

Part of the book series: Receptor Purification ((RP,volume 1))

Abstract

Prolactin (PRL), first discovered by Stricker and Grueter (1928), is a protein hormone secreted from the anterior pituitary gland. It is a highly pleiotropic hormone and appears in all vertebrates. Nicoll and Bern (1972) have listed over 85 different biological activities attributable to PRL. The outstanding of these include lactation and reproduction in mammals and regulation of water and ion fluxes in amphibians and fish. PRL receptors have been identified in various tissues of mammals and in the livers and kidneys of fish and amphibians. Nicoll et al. (1986) recently published an extensive review devoted to the analysis of relations beween prolactins, growth hormones, and their receptors. Other recent reviews (Kelly et al., 1984; Akers, 1985; Nicoll and White, 1985; Forsyth, 1986; Rillema et al., 1988) have focused on the mechanism of PRL action and the regulation and evolution of PRL receptors. Since these subjects are beyond the scope of the present review, we shall attempt to summarize our present knowledge on purification of prolactin receptors with emphasis on their molecular weight and specificity.

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Authors
  1. Arieh Gertler
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Editors and Affiliations

  1. Fels Institute for Cancer Research and Molecular Biology, Philadelphia, PA, USA

    Gerald Litwack

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© 1990 Springer Science+Business Media New York

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Gertler, A. (1990). Prolactin Receptors. In: Litwack, G. (eds) Receptor Purification. Receptor Purification, vol 1. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-4612-0461-9_13

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  • DOI: https://doi.org/10.1007/978-1-4612-0461-9_13

  • Publisher Name: Humana Press, Totowa, NJ

  • Print ISBN: 978-1-4612-6771-3

  • Online ISBN: 978-1-4612-0461-9

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