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Glutathione and γ-glutamylcysteine in hydrogen peroxide detoxification

AuthorsQuintana-Cabrera, Ruben; Bolaños, Juan P.
Glutathione peroxidase-1
Issue Date2013
CitationMethods in Enzymology 527(Cap. 7): 129-144 (2013)
SeriesHydrogen Peroxide and cell signaling, Part B
AbstractHydrogen peroxide (H2O2) is an important regulator of cell redox status and signaling pathways. However, if produced in excess, it can trigger oxidative damage, which can be counteracted by the antioxidant systems. Amongst these, the glutathione (GSH) precursor, γ- glutamylcysteine (γGC), has recently been shown to detoxify H 2O2 in a glutathione peroxidase-1 (GPx1)-dependent fashion. To analyze how both γGC and GSH reduce H2O 2, we have taken advantage of a colorimetric assay that allows simple and reliable quantification of H2O2 in the micromolar range. Whereas most assays rely on coupled enzymatic reactions, this method determines the formation of a ferric thiocyanate derivative after direct Fe 2 + oxidation by H2O2. Here, we detail the procedure and considerations to determine H2O2 reduction by both γGC and GSH, either from cell samples or in vitro reactions with purified enzymes from GSH metabolism. © 2013 Elsevier Inc.
Identifiersdoi: 10.1016/B978-0-12-405882-8.00007-6
isbn: 978-0-12-405882-8
Appears in Collections:(IBFG) Libros y partes de libros
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