Prompted by the recently reported capacity of the physiologically occurring Cu(I)-[glutathione]2 complex (Cu(I)-[GSH)]2) to reduce oxygen, the effect of various GSH-binding metals (Co2+, Cd2+, Zn2+, Pb2+, Al3+, Hg2+ and ...

Glutathione is an important intracellular tripeptide with multiple functions. Abnormal glutathione metabolism is thought to play an important role in various diseases of cats. However, no data regarding concentration of ...

Background: Glutathione (GSH) is one of the most important agents of the antioxidant defense system of the cell because, in conjunction with the enzymes glutathione peroxidase (GSH-Px) and glutathione S transferase pi ...

Binding of copper by reduced glutathione (GSH) is generally seen as a mechanism to lower, if not abolish, the otherwise high electrophilicity and redox activity of its free ions. In recent years, however, this concept has ...

The interaction between Cu2+ ions and GSH molecules leads to the swift formation of the physiologically occurring Cu(I)-[GSH](2) complex. Recently, we reported that this complex is able to reduce molecular oxygen into ...

The intracellularly-occurring Cu(I)-glutathione complex (Cu(I)-[GSH] 2) has the ability to reduce molecular oxygen into superoxide. Removal of such radicals leads to the irreversible conversion of Cu(I)-[GSH] 2 into the ...

Several components of the erythrocyte-dependent glutathione redox system (reduced glutathione, GSH; oxidized glutathione, GSSG; glutathione peroxidase, GSH-Px; glutathione reductase, GSH-Red) were determined in patients ...