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Levels of glutathione, glutathione reductase and glutathione S-transferase activities in rat lung and liver.
Levels of glutathione, glutathione reductase and glutathione S-transferase activities in rat lung and liver have been investigated. After perfusing the lung to remove contaminating blood, this organ… Expand
 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 maintenance… Expand
Purification and characterization of the flavoenzyme glutathione reductase from rat liver.
Glutathione reductase from rat liver has been purified greater than 5000-fold in a yield of 20%. The molecular weights of the enzyme and its subunits were estimated to be 125,000 and 60,000,… Expand
Glutathione transferase (human placenta).
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 numerous… Expand
 Glutathione transferase (human placenta)
Publisher Summary Glutathione transferases with basic isoelectric points have been purified from the human liver, and an acidic form is purified from human erythrocytes. However, this chapter… Expand
The isoenzymes of glutathione transferase.
- B. Mannervik
- Medicine, Chemistry
- 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.
- K. Berhane, M. Widersten, A. Engström, J. Kozarich, B. Mannervik
- Chemistry, Medicine
- Proceedings of the National Academy of Sciences…
- 15 February 1994
Radiation and chemical reactions that give rise to free radicals cause the formation of highly cytotoxic base propenals, degradation products of DNA. Human glutathione transferases (GSTs;… Expand
Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue.
BACKGROUND Glyoxalase II, the second of two enzymes in the glyoxalase system, is a thiolesterase that catalyses the hydrolysis of S-D-lactoylglutathione to form glutathione and D-lactic acid. … Expand