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NAD+ Biosynthesis in Human Placenta: Characterization of Homogeneous NMN Adenylyltransferase

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ADP-Ribosylation Reactions

Abstract

The nuclear location of NMN adenylyltransferase (NMNAT), the last enzyme in the main biosynthetic pathway of NAD+, prompted us to investigate about a possible involvement of this enzyme in the regulation of the cellular activity by hypothesizing its eventual relationship with poly(ADP-ribose) polymerase (ADPRP), another chromatin bound enzyme. This hypothesis was based on the discovery of an inhibitory effect exerted by NMNAT on ADPRP in vitro in reconstituted systems, composed by enzymes purified both from different sources (heterologous system) (1) and from identical sources (homologous system) (2). In order to verify such a phenomenon in man and to better elucidate its functional significance we carried out the purification of NMNAT from human placenta, where the system involved in NAD+ comsumption has been fully characterized (3).

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References

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Authors
  1. M. Emanuelli
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  2. N. Raffaelli
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  3. S. Ruggieri
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  4. E. Balducci
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  5. P. Natalini
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  6. G. Magni
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Editor information

Editors and Affiliations

  1. Centre de Recherches en Endocrinologie Moleculaire, Le Centre Hospitalier de l’Universite Laval, Quebec, G1V 4G2, Canada

    Guy G. Poirier

  2. Biochemistry Department Pavillon Vachon, Universite Laval, Quebec, G1K 7P4, Canada

    Pierre Moreau

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© 1992 Springer Science+Business Media New York

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Emanuelli, M., Raffaelli, N., Ruggieri, S., Balducci, E., Natalini, P., Magni, G. (1992). NAD+ Biosynthesis in Human Placenta: Characterization of Homogeneous NMN Adenylyltransferase. In: Poirier, G.G., Moreau, P. (eds) ADP-Ribosylation Reactions. Springer, New York, NY. https://doi.org/10.1007/978-1-4419-8718-1_74

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  • DOI: https://doi.org/10.1007/978-1-4419-8718-1_74

  • Publisher Name: Springer, New York, NY

  • Print ISBN: 978-1-4612-6456-9

  • Online ISBN: 978-1-4419-8718-1

  • eBook Packages: Springer Book Archive

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