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Purification and Characterization of Acidic Glutathione S-Transferases (EC 2.5.1.18) from Rat Kidney

  • F. J. Romero
  • I. Gath
  • H. Thomas
  • U. Milbert
  • F. Oesch
Part of the Archives of Toxicology book series (TOXICOLOGY, volume 12)

Abstract

Glutathione S-transferases (EC 2.5.1.18) (GSTs) are present in almost every mammalian tissue and catalyze the conjugation of glutathione (GSH) with different electrophilic substrates (Habig et al. 1974). In contrast to this deactivation function of GSTs, they also appear to be involved in the activation of certain chemicals, and particularly halogenated compounds, in either the liver or extra-hepatic tissues (even the kidney) to nephrotoxic and potentially nephrocarcin-ogenic products (Anders et al. 1987, Dekant et al. 1986, Elfarra and Anders 1984, Igwe 1986). These previous results confirm the necessity of a deeper insight into the GSH conjugation system of the kidney: firstly, because of the possible nephrotoxic effects of certain compounds resulting from the above-mentioned conjugation reaction; secondly, because kidneys receive blood which may contain “natural” substrates for GSTs, among others 4-hydroxyalk-2-enals. These are toxic products of lipid peroxidation (Esterbauer 1982).

Keywords

Glutathione Transferase Mercapturic Acid Electrophilic Substrate Pool Active Fraction Activity Activity Activity 
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 1988

Authors and Affiliations

  • F. J. Romero
    • 1
  • I. Gath
    • 1
  • H. Thomas
    • 1
  • U. Milbert
    • 2
  • F. Oesch
    • 1
  1. 1.Institut für ToxikologieUniversität MainzMainzGermany
  2. 2.Toxikologie und PathologieHoechst AG Pharma ForschungFrankfurt a. M. 80Germany

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