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Levels of glutathione, glutathione reductase and glutathione S-transferase activities in rat lung and liver.
The activities of some glutathione-metabolizing enzymes were observed to be 5-to 60-fold lower in lung tissue than in the liver, and that phenobarbital nor methylcholanthrene had a significant effect on the levels of reduced glutATHione in lung and liver. Expand
[59] Glutathione reductase
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 maintenanceExpand
Purification and characterization of the flavoenzyme glutathione reductase from rat liver.
The steady state kinetic data are consistent with a branching reaction mechanism previously proposed for glutathione reductase from yeast, and at low GSSG concentrations the rate equation can be approximated by that of a simple ping pong mechanism. Expand
Glutathione transferases--structure and catalytic activity.
The glutathione transferases are recognized as important catalysts in the biotransformation of xenobiotics, including drugs as well as environmental pollutants. Multiple forms exist, and numerousExpand
The isoenzymes of glutathione transferase.
  • B. Mannervik
  • Chemistry, Medicine
  • Advances in enzymology and related areas of…
  • 22 November 2006
Detoxication of base propenals and other alpha, beta-unsaturated aldehyde products of radical reactions and lipid peroxidation by human glutathione transferases.
The results show that glutathione transferases may play an important role in cellular detoxication of electrophilic alpha, beta-unsaturated carbonyl compounds produced by radical reactions, lipid peroxidation, ionizing radiation, and drug metabolism. Expand
Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue.
The structure of human glyoxalase II was solved initially by single isomorphous replacement with anomalous scattering and refined at a resolution of 1.9 A, and the reaction mechanism may also have implications for the action of metallo-beta-lactamases. Expand
Identification of three classes of cytosolic glutathione transferase common to several mammalian species: correlation between structural data and enzymatic properties.
It is suggested that the similarities of the isoenzymes in a class reflect evolutionary relationships and that the classification applies generally. Expand
Human glutathione transferase A4-4: an alpha class enzyme with high catalytic efficiency in the conjugation of 4-hydroxynonenal and other genotoxic products of lipid peroxidation.
4-Hydroxynonenal and other reactive electrophiles produced by oxidative metabolism have been linked to aging, atherosclerosis, cataract formation, Parkinson's disease and Alzheimer's disease, as well as other degenerative human conditions, suggesting that human GST A4-4 fulfills an important protective role and that variations in its expression may have significant pathophysiological consequences. Expand
4‐Hydroxyalk‐2‐enals are substrates for glutathione transferase
It is proposed that a major biological function of the glutathione transferases is to protect the cell against products of oxidative metabolism, such as epoxides, organic hydroperoxide, and 4‐hydroxyalkenals. Expand