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ADP-Ribosylation of Proteins in Normal and Neoplastic Tissues

  • Helmuth Hilz
  • Peter Adamietz
  • Reinhard Bredehorst
  • Klaus Wielckens
Part of the NATO Advanced Science Institutes Series book series (NSSA, volume 57)

Abstract

In 1966, Mandel and coworkers in Strasbourg described an enzyme located in the nucleus of chicken liver, which is able to transfer active ADPR groups from NAD to form a homopolymer (1). In this polymer ADPR residues are linked O-glycosidically. Shortly later, Hayaishi and coworkers (2) as well as Sugimura’s group (3) reported on similar findings. Recent evidence indicates that the structure can also be branched (4). The nuclear ADPR transferase is apparently present in all eukaryotes (5–7). It differs basically from ADPR transferase subsequently found to be associated with certain bacterial toxins and with phages: The prokaryotic enzymes transfer single ADPR residues either to one acceptor protein as in the case of Diphteria toxin, where the ribosomal elongation factor 2 is the target (8), or to multiple proteins which serve as acceptors of the T4 and the N4 phage-induced ADPR transferase (cf. 5–7). By contrast, the nuclear enzyme forms preferentially oligo- and poly(ADPR) conjugates with various protein acceptors.

Keywords

Chronic Lymphocytic Leukemia NEOPLASTIC Tissue Protein Conjugate Acceptor Protein Histone Fraction 
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 Science+Business Media New York 1983

Authors and Affiliations

  • Helmuth Hilz
    • 1
  • Peter Adamietz
    • 1
  • Reinhard Bredehorst
    • 1
  • Klaus Wielckens
    • 1
  1. 1.Institut für Physiologische ChemieUniversität HamburgGermany

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