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Characterization of NAD: Arginine Mono(ADP-Ribosyl)-Transferases in Turkey Erythrocytes: Determinants of Substrate Specificity

  • Joel Moss
  • Robert E. WestJr.
  • James C. OsborneJr.
  • Rodney L. Levine
Part of the Proceedings in Life Sciences book series (LIFE SCIENCES)

Abstract

Mono(ADP-ribosylation) is catalyzed by transferases identified in viruses, bacteria, and animal cells [1]. Its function has thus far been clearly defined only for certain bacterial toxins that exert their effects on animal tissues by catalyzing the mono(ADP-ribosylation) of critical cellular proteins [1–5]. One of these toxins, choleragen (cholera toxin), an NAD:arginine mono(ADP-ribosyl)transferase, causes the activation of the hormone-sensitive adenylate cyclase from animal tissues by ADP-ribosylating a guanine nucleotide-binding stimulatory protein termed Gs [5]. In vitro, choleragen also catalyzes the ADP-ribosylation of several proteins not related to the cyclase system as well as low molecular weight guanidino compounds, such as the amino acid arginine [6–8]. Animal tissues contain NAD:arginine (ADP-ribosyl)transferases that catalyze reactions similar to those of choleragen [7, 9–11].

Keywords

Glutamine Synthetase Carbamyl Phosphate Amino Acid Arginine Chaotropic Salt Carbamyl Phosphate Synthetase 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag Berlin Heidelberg 1985

Authors and Affiliations

  • Joel Moss
  • Robert E. WestJr.
  • James C. OsborneJr.
  • Rodney L. Levine
    • 1
  1. 1.National Heart, Lung, and Blood InstituteNational Institutes of HealthBethesdaUSA

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