Glutathione: Research, Handling and Batch Documentation

Identity and research status

Also referred to as

GSH, L-Glutathione, Gamma-Glutamylcysteinylglycine, Reduced Glutathione

Sequence

gamma-L-Glu-L-Cys-Gly (gamma-glutamyl isopeptide linkage, not a standard alpha peptide bond)

IUPAC Name

(2S)-2-amino-5-[[(2R)-1-(carboxymethylamino)-1-oxo-3-sulfanylpropan-2-yl]amino]-5-oxopentanoic acid

Molecular Formula

C10H17N3O6S

Molecular Weight

307.32 g/mol (monoisotopic 307.0838)

CAS Number

70-18-8

PubChem CID

124886

InChIKey

RWSXRVCMGQZWBV-WDSKDSINSA-N

SMILES

C(CC(=O)NC(CS)C(=O)NCC(=O)O)C(C(=O)O)N

ChEBI ID

CHEBI:16856

XLogP

-4.5 (strongly hydrophilic: two carboxylates, one amine and a free thiol)

Topological Polar Surface Area

160 square angstroms

Oxidised Form (GSSG)

Glutathione disulfide, C20H32N6O12S2, 612.6 g/mol, PubChem CID 65359

Common Synonyms

GSH, L-glutathione reduced, gamma-glutamylcysteinylglycine, Tathion, Tathione

Appearance

White to off-white lyophilized powder, freely soluble in water

Mechanism, in brief

Glutathione has no receptor. It is not a signalling peptide in the sense that the rest of a peptide catalogue is, and looking for a binding site is the wrong model. Its activity comes entirely from the sulfhydryl group on the cysteine residue, which is a good nucleophile and a good one-electron and two-electron donor at physiological pH. Everything the molecule does follows from that thiol: reduction of peroxides, conjugation to electrophiles, reversible modification of protein cysteines, and coordination of metals.

1. Thiol donation. The cysteine sulfhydryl donates reducing equivalents to peroxides, radicals and oxidised protein thiols. Two molecules of GSH are consumed per disulfide formed, which is why the redox potential depends on the square of the reduced concentration.
2. Peroxide reduction. Glutathione peroxidases, selenocysteine enzymes since Rotruck's 1973 work, use GSH to reduce hydrogen peroxide and lipid hydroperoxides. GPX4 is the isoform that acts on phospholipid hydroperoxides inside membranes.
3. Electrophile conjugation. Glutathione S-transferases catalyse addition of the thiolate to electrophilic centres, forming glutathione conjugates that MRP-family transporters pump out of the cell for downstream processing to mercapturic acids.
4. Regeneration by glutathione reductase. GSSG is reduced back to two GSH at the expense of NADPH from the pentose phosphate pathway, closing the cycle. More than 98 percent of cellular glutathione sits in the reduced form when this cycle is keeping up.
5. Extracellular breakdown by gamma-glutamyl transpeptidase. The isopeptide bond blocks ordinary aminopeptidases, so degradation begins only after export, at the cell surface, where GGT transfers the gamma-glutamyl group to an acceptor amino acid and releases cysteinylglycine.
6. Mitochondrial import. No glutathione is made inside mitochondria. The 10 to 15 percent of the cellular pool held there is imported across the inner membrane by SLC25A39 and its paralogue SLC25A40, identified in 2021.

The full research write-up, including the findings behind each claim and the model each came from, is on the Glutathione 1500mg 1,500mg page.

Vial sizes available

Every size of Glutathione Volta lists, in stock or not. Each is a separate catalogue page with its own batch number and specification table.

• Glutathione 1500mg 1,500mgBatch #: VPGT1500100
  Restocking

Purity and batch documentation

Volta's release specification is >99% (HPLC). That is a threshold we set. >99% is the specification every batch is released to. The figure on a certificate is what a laboratory measured for one lot.

No third-party certificate has been published for Glutathioneyet. The certificates Volta does publish, with the laboratory's own verification link on each, are in the certificate archive.

Research on Glutathione

Handling and stability

Regulatory context

United States

Available as dietary supplement (oral); injectable forms used in clinical practice but not FDA-approved as a drug. Compounding pharmacies provide SC/IV formulations.

Japan

Approved pharmaceutical (Tathion) for drug-induced liver damage and other indications.

Europe

Available as supplement; IV use in clinical settings.

• the legal status of research peptides in Canada
• Health Canada's regulatory position

Primary sources

1. Meister A, Anderson ME. Glutathione. Annual Review of Biochemistry (1983). doi:10.1146/annurev.bi.52.070183.003431
2. Orlowski M, Meister A. The gamma-glutamyl cycle: a possible transport system for amino acids. Proceedings of the National Academy of Sciences (1970). doi:10.1073/pnas.67.3.1248
3. Harington CR, Mead TH. Synthesis of glutathione. Biochemical Journal (1935)
4. Lu SC. Glutathione synthesis. Biochimica et Biophysica Acta (2013). doi:10.1016/j.bbagen.2012.09.008
5. Schafer FQ, Buettner GR. Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radical Biology and Medicine (2001). doi:10.1016/s0891-5849(01)00480-4
6. Hwang C, Sinskey AJ, Lodish HF. Oxidized redox state of glutathione in the endoplasmic reticulum. Science (1992). doi:10.1126/science.1523409
7. Mills GC. Hemoglobin catabolism. I. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidative breakdown. Journal of Biological Chemistry (1957). PMID 13491573
8. Rotruck JT, Pope AL, Ganther HE, Swanson AB, Hafeman DG, Hoekstra WG. Selenium: biochemical role as a component of glutathione peroxidase. Science (1973). doi:10.1126/science.179.4073.588
9. Yang WS, SriRamaratnam R, Welsch ME, et al.. Regulation of ferroptotic cancer cell death by GPX4. Cell (2014). doi:10.1016/j.cell.2013.12.010
10. Lieberman MW, Wiseman AL, Shi ZZ, et al.. Growth retardation and cysteine deficiency in gamma-glutamyl transpeptidase-deficient mice. Proceedings of the National Academy of Sciences (1996). doi:10.1073/pnas.93.15.7923
11. Dalton TP, Dieter MZ, Yang Y, Shertzer HG, Nebert DW. Knockout of the mouse glutamate cysteine ligase catalytic subunit (Gclc) gene: embryonic lethal when homozygous, and proposed model for moderate glutathione deficiency when heterozygous. Biochemical and Biophysical Research Communications (2000). doi:10.1006/bbrc.2000.3930
12. Meredith MJ, Reed DJ. Status of the mitochondrial pool of glutathione in the isolated hepatocyte. Journal of Biological Chemistry (1982). PMID 7061508
13. Griffith OW, Meister A. Origin and turnover of mitochondrial glutathione. Proceedings of the National Academy of Sciences (1985). doi:10.1073/pnas.82.14.4668
14. Wang Y, Yen FS, Zhu XG, et al.. SLC25A39 is necessary for mitochondrial glutathione import in mammalian cells. Nature (2021). doi:10.1038/s41586-021-04025-w
15. Shi X, Reinstadler B, Shah H, et al.. Combinatorial GxGxE CRISPR screen identifies SLC25A39 in mitochondrial glutathione transport linking iron homeostasis to OXPHOS. Nature Communications (2022). doi:10.1038/s41467-022-30126-9
16. Witschi A, Reddy S, Stofer B, Lauterburg BH. The systemic availability of oral glutathione. European Journal of Clinical Pharmacology (1992). doi:10.1007/BF02284971
17. Richie JP Jr, Nichenametla S, Neidig W, et al.. Randomized controlled trial of oral glutathione supplementation on body stores of glutathione. European Journal of Nutrition (2015). doi:10.1007/s00394-014-0706-z
18. Allen J, Bradley RD. Effects of oral glutathione supplementation on systemic oxidative stress biomarkers in human volunteers. Journal of Alternative and Complementary Medicine (2011). doi:10.1089/acm.2010.0716
19. Sinha R, Sinha I, Calcagnotto A, et al.. Oral supplementation with liposomal glutathione elevates body stores of glutathione and markers of immune function. European Journal of Clinical Nutrition (2018). doi:10.1038/ejcn.2017.132
20. Sonthalia S, Jha AK, Lallas A, Jain G, Jakhar D. Glutathione for skin lightening: a regnant myth or evidence-based verity?. Dermatology Practical and Conceptual (2018). doi:10.5826/dpc.0801a04
21. Arjinpathana N, Asawanonda P. Glutathione as an oral whitening agent: a randomized, double-blind, placebo-controlled study. Journal of Dermatological Treatment (2012). doi:10.3109/09546631003801619
22. Weschawalit S, Thongthip S, Phutrakool P, Asawanonda P. Glutathione and its antiaging and antimelanogenic effects. Clinical, Cosmetic and Investigational Dermatology (2017). doi:10.2147/CCID.S128339
23. Marrades RM, Roca J, Barbera JA, de Jover L, MacNee W, Rodriguez-Roisin R. Nebulized glutathione induces bronchoconstriction in patients with mild asthma. American Journal of Respiratory and Critical Care Medicine (1997). doi:10.1164/ajrccm.156.2.9611001
24. Rossi R, Dalle-Donne I, Milzani A, Giustarini D. Oxidized forms of glutathione in peripheral blood as biomarkers of oxidative stress. Clinical Chemistry (2006). doi:10.1373/clinchem.2006.067793
25. Honda Y, Kessoku T, Sumida Y, et al.. Efficacy of glutathione for the treatment of nonalcoholic fatty liver disease: an open-label, single-arm, multicenter, pilot study. BMC Gastroenterology (2017). doi:10.1186/s12876-017-0652-3
26. Mischley LK, Lau RC, Shankland EG, Wilbur TK, Padowski JM. Phase IIb study of intranasal glutathione in Parkinson's disease. Journal of Parkinson's Disease (2017). doi:10.3233/JPD-161040
27. National Center for Biotechnology Information. Glutathione, PubChem Compound Summary CID 124886. PubChem (2026)