/pdf/glutathione-s-transferases-as-biomarkers-of-organ-damage-ywqs7z6xet.pdf

Glutathione S-transferases as biomarkers of organ damage: applications of rodent and canine GST enzyme immunoassays.

Glutathione S-transferases (GSTs) play critical roles in detoxification, response to oxidative stress, regeneration of S-thiolated proteins, and catalysis of reactions in nondetoxification metabolic pathways. Liver GSTs were purified from the anoxia-tolerant turtle, Trachemys scripta elegans. Purification separated a homodimeric (subunit relative molecular mass =34 kDa) and a heterodimeric (subunit relative molecular mass = 32.6 and 36.8 kDa) form of GST. The enzymes were purified 23–69-fold and 156–174-fold for homodimeric and heterodimeric GSTs, respectively. Kinetic data gathered using a variety of substrates and inhibitors suggested that both homodimeric and heterodimeric GSTs were of the α class although they showed significant differences in substrate affinities and responses to inhibitors. For example, homodimeric GST showed activity with known α class substrates, cumene hydroperoxide and p-nitrobenzylchloride, whereas heterodimeric GST showed no activity with cumene hydroperoxide. The specific activity of liver GSTs with chlorodinitrobenzene (CDNB) as the substrate was reduced by 2.6- and 8.7-fold for homodimeric and heterodimeric GSTs isolated from liver of anoxic turtles as compared with aerobic controls, suggesting an anoxia-responsive stable modification of the protein that may alter its function during natural anaerobiosis.

https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/j.1742-4658.2005.04783.x

Purification and properties of the glutathione S-transferases from the anoxia-tolerant turtle, Trachemys scripta elegans

Characterization of multiple Chinese hamster carbonyl reductases

A lens glutathione S-transferase, class mu, with thiol-specific antioxidant activity.

Further characterization of Chinese hamster carbonyl reductases (CHCRs)

Purification and characterization of glutathione s-transferase isozymes in dog lens

Purification and characterization of carbonyl reductases from bovine liver cytosol and microsome. the cytosolic enzyme has a novel 3α/17β-hydroxysteroid dehydrogenase activity

Terada Tomoyuki

Papers

Purification and characterization of glutathione s-transferase isozymes in dog lens

Purification and characterization of carbonyl reductases from bovine liver cytosol and microsome. the cytosolic enzyme has a novel 3α/17β-hydroxysteroid dehydrogenase activity