Glutathione (L-Glutathione Reduced)

Glutathione (L-glutathione reduced, γ-L-glutamyl-L-cysteinyl-glycine) is the most abundant intracellular antioxidant in mammalian cells, present at concentrations of 1-10 mM. This tripeptide serves as the primary substrate for glutathione peroxidase and glutathione S-transferase enzyme families, and is essential for Phase II detoxification, xenobiotic metabolism, and maintenance of intracellular redox balance. The reduced thiol group on its cysteine residue provides the electron-donating capacity central to its antioxidant function.

Key Research Findings:

• Intracellular depletion studies demonstrated direct correlation between GSH levels and oxidative stress biomarkers (MDA, 8-OHdG, protein carbonyls)
• In vitro research showed glutathione recycling via glutathione reductase (GR) maintains a >100:1 GSH:GSSG ratio in healthy cells
• Preclinical models demonstrated that GSH is critical for cytochrome P450-mediated Phase I and conjugation-dependent Phase II detoxification pathways
• Cell culture studies confirmed glutathione's role as a cofactor for glutathione peroxidase (GPx), neutralizing H₂O₂ and lipid hydroperoxides

For laboratory and research use only.