Glutathione

Third-Party Tested

Independent lab verified

Batch-Specific CoA

Publicly accessible

YPB.259

Reference number

1500mg

Lyophilized vial

Origin

Glutathione was first identified by Frederick Gowland Hopkins in 1921 at Cambridge University. Hopkins isolated the compound from yeast and recognized it as a dipeptide, though its correct tripeptide structure (gamma-glutamyl-cysteinyl-glycine) was established by Harington and Mead in 1935. It is the most abundant non-protein thiol in mammalian cells.

Research Lineage

Meister and Anderson at Cornell University Medical College conducted foundational work on the gamma-glutamyl cycle and glutathione metabolism in the 1980s. Lu at the USC Keck School of Medicine has published extensively on hepatic glutathione regulation. Over 170,000 PubMed entries reference glutathione, making it one of the most studied molecules in biochemistry.

Mechanism of Action

Glutathione functions as the principal intracellular redox buffer, cycling between reduced (GSH) and oxidized (GSSG) forms via glutathione peroxidase and glutathione reductase. It serves as a cofactor for glutathione S-transferases in phase II detoxification, conjugating electrophilic xenobiotics for excretion. It also maintains protein thiol status and regenerates other antioxidants including vitamins C and E.

Structural Notes

Tripeptide. Sequence: gamma-L-Glutamyl-L-Cysteinyl-Glycine. Molecular weight: 307.32 Da. The gamma peptide bond (via glutamate side chain) confers resistance to normal peptidases. The cysteine thiol group (-SH) is the active functional group.