Purification and Characterization of Acidic Glutathione S-Transferases (EC 184.108.40.206) from Rat Kidney
Glutathione S-transferases (EC 220.127.116.11) (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).
KeywordsCellulose Glutathione Cysteine Fluor Cytosol
Unable to display preview. Download preview PDF.
- Dekant W, Metzler M, Henschler D (1986) Identification of S-l,2,2-trichlorovinyl-N-acetyl-cysteine as a urinary metabolite of tetrachloroethylene: bioactivation through glutathione conjugation as a possible explanation of its nephrocarcinogenicity. J Biochem Toxicol 1:57 – 72PubMedCrossRefGoogle Scholar
- Esterbauer H (1982) Aldehydic products of lipid peroxidation. In: McBrien DCH, Slater TF (eds) Free radicals, lipid peroxidation and cancer. Academic, London, pp 101–128Google Scholar
- Milbert U, Wörner W, Oesch F (1986) Characterization of rat hepatic and renal glutathione S-transferases. In: Friedberg T, Oesch F (eds) Primary changes and control factors in carcinogenesis. Deutscher Fachschriften-Verlag, Wiesbaden, pp 14–21Google Scholar