Glutathione — 1200mg

Glutathione (γ-L-glutamyl-L-cysteinyl-glycine) is a tripeptide synthesized intracellularly from glutamate, cysteine, and glycine by the sequential action of γ-glutamylcysteine synthetase and glutathione synthetase. It is present at millimolar concentrations in every human cell, making it the most abundant intracellular antioxidant and the principal regulator of cellular redox state. Its unique γ-glutamyl linkage — rather than the standard α-peptide bond between Glu and Cys — confers resistance to most peptidases and extends its intracellular half-life substantially.

The molecule cycles between its reduced (GSH) and oxidized (GSSG) forms, donating electrons to neutralize reactive oxygen species (ROS) either directly or through glutathione peroxidase-catalyzed reactions. Glutathione is also the obligate substrate for glutathione S-transferases (GSTs), the enzyme family responsible for phase II hepatic detoxification — conjugating GSH to electrophilic xenobiotics, heavy metals, and endogenous toxins to render them water-soluble and excretable. The GSH:GSSG ratio is a widely used biomarker of cellular oxidative stress, with depletion implicated in neurodegeneration, hepatic injury, and immune dysfunction.

Research applications include studies of hepatic detoxification pathways, oxidative stress-related disease models, mitochondrial dysfunction, immune cell redox signaling, and skin depigmentation research (via inhibition of tyrosinase-mediated melanogenesis). Intravenous and subcutaneous glutathione research protocols have examined its effects on Parkinson's disease, hepatic disease, chemotherapy tolerance, and dermatological endpoints. Because oral glutathione is extensively degraded by intestinal peptidases, parenteral administration is the standard route for research involving direct intracellular replenishment.