Topic
Glutathione
About: Glutathione is a research topic. Over the lifetime, 42523 publications have been published within this topic receiving 1876505 citations. The topic is also known as: GSH & Glutathione-SH.
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TL;DR: A dose threshold exists for bromobenzene-induced hepatic necrosis and it is demonstrated that the hepatotoxic metabolite is preferentially conjugated (detoxified) with glutathione, thereby depleting glutATHione from the liver.
Abstract: This laboratory has previously postulated that bromobenzene-induced hepatic necrosis results from the formation of a reactive metabolite that arylates vital cellular macromolecules. Accordingly, the severity of liver necrosis has been compared with the formation of metabolites of bromobenzene and with covalent binding of metabolites in vivo and in vitro after various pretreatment regimens that alter hepatotoxicity. These data provide direct kinetic evidence that 3,4-bromobenzene oxide is the reactive hepatotoxic metabolite. The studies also demonstrate that the hepatotoxic metabolite is preferentially conjugated (detoxified) with glutathione, thereby depleting glutathione from the liver. Liver necrosis and arylation of cellular macromolecules occur only when glutathione is no longer available. Thus, a dose threshold exists for bromobenzene-induced hepatic necrosis.
2,822 citations
TL;DR: This chapter presents a procedure for the preparation of glutathione peroxidase, which is regarded as a major protective system against endogenously and exogenously induced lipid peroxidation.
Abstract: Publisher Summary This chapter presents a procedure for the preparation of glutathione peroxidase, which is regarded as a major protective system against endogenously and exogenously induced lipid peroxidation. Two types of methods are used for determining the activity of glutathione peroxidase. One involves a direct measurement of unconsumed glutathione (GSH) at fixed time periods by polarographic GSH analysis' (Method 1), or by the dithionitrobenzoic acid method (Method 2). The second approach takes advantage of the capability of glutathione reductase, with nicotinamide adenine dinucleotide phosphate (NADPH), to regenerate GSH from oxidized GSH. The decrease in NADPH is continuously measured spectrophotometrically, while the GSH concentration in the enzymatic cycle remains essentially constant (Method 3). A convenient source for the preparation of glutathione peroxidase is bovine blood including the following steps: hemolysate; organic solvent precipitation; phosphate precipitation; absorption to phenyl-sepharose; and washing on diethylaminoethyl (DEAE)–sephadex, S-300 sephacryl, and hydroxylapatite column.
2,809 citations
TL;DR: It is reported here that H2O2 from this oxidative burst not only drives the cross-linking of cell wall structural proteins, but also functions as a local trigger of programmed death in challenged cells and as a diffusible signal for the induction in adjacent cells of genes encoding cellular protectants.
2,740 citations
TL;DR: 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB)-GSSG reductase recycling assay for total glutathione is a specific, sensitive, rapid, and reliable procedure, however, because the method depends on an accurate standard curve, appropriate standards containing the protein precipitating agent are essential.
Abstract: Publisher Summary There are a number of procedures, for example, chemical, enzymatic, and chromatographic for the determination of glutathione (GSH) and glutathione disulfide (GSSG) in biological samples. Enzymatic and chromatographic methods for the determination of glutathione in biological samples are described in this chapter. Because GSH readily oxidizes nonenzymatically and because it is a good substrate of γ-glutamyl transpeptidase, the biological samples are acidified quickly to reduce oxidation of GSH to GSSG and to mixed disulfides, and to inactivate γ-glutamyl transpeptidase. Glutathione oxidizes rapidly at pH values greater than 7. Acid treatment inactivates γ-glutamyl transpeptidase, which catalyzes the reactions that decrease the levels of both GSH and GSSG. The optimum method for treating biological samples depends upon the tissue and the experimental system. The discussed 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB)-GSSG reductase recycling assay for total glutathione is a specific, sensitive, rapid, and reliable procedure. However, because the method depends on an accurate standard curve, appropriate standards containing the protein precipitating agent are essential.
2,623 citations
TL;DR: A purification method of glutathione reductase from calf liver and rat liver is described and it is shown that this enzyme has a major role as a reductant in oxidation–reduction processes, and serves in detoxication and several other cellular functions of great importance.
Abstract: Publisher Summary Glutathione reductase is a flavoprotein catalyzing the NADPH-dependent reduction of glutathione disulfide (GSSG) to glutathione (GSH). The reaction is essential for the maintenance of glutathione levels. Glutathione has a major role as a reductant in oxidation–reduction processes, and serves in detoxication and several other cellular functions of great importance. A purification method of this enzyme from calf liver and rat liver is described in this chapter. Similar methods are used for the purification of the enzyme from yeast, porcine, and human erythrocytes. All the steps are carried out at about 5°. The purification method from calf liver consists of various steps including preparation of cytosol fraction, chromatography on DEAE-sephadex, precipitation with ammonium sulfate, and chromatography on hydroxyapatite. The purification of glutathione reductase from rat liver is usually combined with the preparation of glutathione transferases, thioltransferase, and glyoxalase I.
2,366 citations