The physiological significance of the selenium-independent glutathione peroxidase (GPx)
activity of glutathione S-transferases (GSTs), associated with the major Alpha class …

In order to elucidate the protective role of glutathione S-transferases (GSTs) against
oxidative stress, we have investigated the kinetic properties of the human α-class GSTs …

It has been known that glutathione S-transferases (GSTs) can reduce lipid hydroperoxides
through their Se-independent glutathione peroxidase activity and that these enzymes can …

A 25.5 kDa class alpha glutathione S-transferase (GST) designated as microsomal Ya-GST
or M-GSTA has been purified to electrophoretic homogeneity from human liver microsomes …

This study investigated phospholipid hydroperoxides as substrates for non-selenium GSH
peroxidase (NSGPx), an enzyme also called 1-Cys peroxiredoxin. Recombinant human …

Glutathione S-transferases (GST) are multifunctional proteins. α class GSTs are known to
catalyze glutathione peroxidase reactions, in addition to their major activity, ie, conjugation …

Since our prior work indicated that Se‐dependent cellular glutathione peroxidase (GPX1)
was necessary for protection against paraquat lethality, the present studies were to elucidate …

We have characterized a new selenium-dependent glutathione peroxidase, GSHPx-GI, by
expressing a GSHPx-GI cDNA isolated from human hepatoma HepG2 cells in human …

Human glutathione transferases (GSTs) from Alpha (A), Mu (M) and Theta (T) classes
exhibited glutathione peroxidase activity towards phospholipid hydroperoxide. The specific …

The mammalian alpha-class glutathione S-transferase (GST) isozymes mGSTA4-4, rGSTA4-
4, and hGSTA4-4 are known to utilize 4-hydroxynonenal (4HNE) as a preferred substrate …