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ADP-Ribosyltransferase from Hen Liver Nuclei: Purification, Properties, and Evidence for ADP-Ribosylation-Induced Suppression of Cyclic AMP-Dependent Phosphorylation

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ADP-Ribosylation of Proteins

Part of the book series: Proceedings in Life Sciences ((LIFE SCIENCES))

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Abstract

ADP-ribosyltransferase catalyzes the transfer of the ADP-ribose moiety of NAD to acceptors, as arginine and other guanidino compounds and proteins, and forms mono-(ADP-ribose)-acceptor adducts. In eukaryotes, this enzyme was first detected in turkey erythrocyte by Moss and associates who went on to purify and characterize the enzyme [1].

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References

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Authors and Affiliations

  1. Department of Biochemistry, Shimane Medical University, Izumo 693, Japan

    Makoto Shimoyama, Yoshinori Tanigawa, Takahisa Ushiroyama, Mikako Tsuchiya & Ryoji Matsuura

Authors
  1. Makoto Shimoyama
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  2. Yoshinori Tanigawa
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  3. Takahisa Ushiroyama
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  4. Mikako Tsuchiya
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  5. Ryoji Matsuura
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Editor information

Editors and Affiliations

  1. Institut für Pharmakologie und Biochemie, Veterinärmedizinische Fakultät der Universität, CH-8057, Zürich, Switzerland

    Felix R. Althaus

  2. Physiologisch-chemisches Institut, Universität Hamburg, 2000, Hamburg 20-40, Germany

    Helmuth Hilz

  3. The University of Sussex, Biology Building, Brighton, Sussex, BN1 9QG, England

    Sydney Shall

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© 1985 Springer-Verlag Berlin Heidelberg

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Shimoyama, M., Tanigawa, Y., Ushiroyama, T., Tsuchiya, M., Matsuura, R. (1985). ADP-Ribosyltransferase from Hen Liver Nuclei: Purification, Properties, and Evidence for ADP-Ribosylation-Induced Suppression of Cyclic AMP-Dependent Phosphorylation. In: Althaus, F.R., Hilz, H., Shall, S. (eds) ADP-Ribosylation of Proteins. Proceedings in Life Sciences. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-70589-2_10

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  • DOI: https://doi.org/10.1007/978-3-642-70589-2_10

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-70591-5

  • Online ISBN: 978-3-642-70589-2

  • eBook Packages: Springer Book Archive

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