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Inhibition of nuclear-protein phosphorylation in vitro by beryllium

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Bioscience Reports

Abstract

Endogenous cyclic-nucleotide-independent protein phosphorylation by ATP at pH 6.5 in adult rat liver nuclei in vitro is inhibited by beryllium (Be2+), but under the same conditions nuclear-protein dephosphorylation appears to be insensitive to Be2+. Prior incubation of nuclei with Be2+ is necessary to demonstrate the inhibition of phosphorylation, which increases as the pH is decreased from pH 8.0 to 6.5. The extent of inhibition can be related to the level of nuclear Be2+ binding and, evidence suggests, may be caused by direct or indirect interference by Be2+ with Mg2+ binding sites normally required to facilitate protein phosphorylation.

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Author notes

  1. Betsan E. Williams

    Present address: Blood Pressure Unit, Charing Cross Hospital Medical School, St. Dunstans Road, W6 8RF, London, UK

Authors and Affiliations

  1. MRC Toxicology Unit, Medical Research Council Laboratories, Woodmansterne Road, SM5 4EF, Carshalton, Surrey, UK

    Betsan E. Williams & David N. Skilleter

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  1. Betsan E. Williams
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  2. David N. Skilleter
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Williams, B.E., Skilleter, D.N. Inhibition of nuclear-protein phosphorylation in vitro by beryllium. Biosci Rep 3, 955–962 (1983). https://doi.org/10.1007/BF01140665

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  • DOI: https://doi.org/10.1007/BF01140665

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