Glutathione
Glutathione is a peptide, indexed here under Mitochondrial and longevity-associated peptides.
Identity
| Field | Value |
|---|---|
| Classification | Peptide |
| Primary class | Mitochondrial and longevity-associated peptides |
| CAS registry number | 70-18-8[1] |
| PubChem CID | 124886[1] |
| UniProt accession | Unknown No UniProt query was run in v1. |
| Molecular formula | C10H17N3O6S[1] |
| Molecular weight | 307.33 g/mol[1] |
| Amino-acid sequence | Unknown Not reported by the PubChem property set retrieved for this record; no sequence database query was run in v1. |
| Reported half-life | Unknown No pharmacokinetics source was retrieved in v1. PubChem does not carry half-life as a property, so this is recorded as not yet sourced rather than estimated. |
What the cited literature examines
Glutathione is the endogenous tripeptide gamma-glutamyl-cysteinyl-glycine. It is indexed here because it is searched and sold alongside the longevity-associated peptides, and its retrieved literature is unlike anything else in this dataset: it is dominated by enzymology and assay methods rather than by studies of the peptide as an administered compound. A 1983 Annual Review of Biochemistry article carries the name as its title, and a 2001 Free Radical Biology and Medicine paper describes the redox environment of the cell through the glutathione disulfide and glutathione couple. The Drugs@FDA register returned one application under this name, for an ophthalmic irrigating solution that contains it; that product is recorded in the regulatory status field and is not what this page describes.
The most-cited records are methods and enzymes: 1963, 1969, 1976 and 1980 papers on the determination of blood, total, oxidised and reduced glutathione, a 1974 Journal of Biological Chemistry paper on glutathione S-transferases as the first enzymatic step in mercapturic acid formation, 1967 and 1984 papers on erythrocyte glutathione peroxidase and its assay, a 1973 Science paper on selenium as a component of glutathione peroxidase, and a 1988 Gene paper on single-step purification of polypeptides expressed as glutathione S-transferase fusions.
[3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13]Reported mechanism
An endogenous tripeptide thiol; the retrieved records characterise it as the substrate of glutathione S-transferases and glutathione peroxidase and as the principal determinant of the cellular redox environment.
[9, 4]Stated in the titles of the cited 1974 Journal of Biological Chemistry and 2001 Free Radical Biology and Medicine papers.
Targets named in the cited records: glutathione S-transferases, glutathione peroxidase, cellular redox couple.
FDA application register
A query of the FDA Drugs@FDA application register on 2026-10-09 returned 1 application record(s) for this compound name (including NDA018469, marketed as BSS PLUS). Material supplied as a research chemical is not the subject of those applications and is not an FDA-approved product.[2]
Scope statement: this records the result of a single automated query against the openFDA drugsfda endpoint on the stated date. It is not legal advice and is not a jurisdiction-by-jurisdiction legality assessment.
Retrieved 2026-10-09.
Amounts reported in the cited literature
Unknown. No retrieved record in this dataset states an amount, so none is shown. Where an amount is recorded it is what a named study reported administering in its own stated model, in the past tense, and is not a protocol.
No study-reported dose was taken from a source read in v1. Literature-reported values are only recorded where the retrieved citation metadata states the figure.
Adverse effects reported in the cited literature
Unknown. No retrieved record in this dataset reports an adverse effect for this compound, so no row is shown. Absence of a row records the absence of a retrieved report, nothing more.
No adverse-effect row was taken from a source read in v1. Rows are only recorded with the study model named and the reporting citation attached.
Other names
Glutathione appears under these other names in the cited records or in common usage. Each one resolves to this page rather than to a separate page of its own.
- GSH
- reduced glutathione
- gamma-glutamyl-cysteinyl-glycine
Where this page sits
Research records
Cited research records for Glutathione, each with its identifier, the publication type it is indexed as, and the study model stated by its assigned subject headings.
Compounds indexed next to it
- Carnosine — Mitochondrial and longevity-associated peptides
- Elamipretide — Mitochondrial and longevity-associated peptides
Class page: Mitochondrial and longevity-associated peptides. Full index: all indexed compounds.
Questions this page answers
What does the cited literature examine for Glutathione?
Glutathione is the endogenous tripeptide gamma-glutamyl-cysteinyl-glycine. It is indexed here because it is searched and sold alongside the longevity-associated peptides, and its retrieved literature is unlike anything else in this dataset: it is dominated by enzymology and assay methods rather than by studies of the peptide as an administered compound.
Which class is Glutathione indexed under?
Glutathione is indexed under Mitochondrial and longevity-associated peptides. This class groups peptides whose retrieved literature concerns mitochondrial function or ageing endpoints.
What does the FDA application register show for Glutathione?
A query of the FDA Drugs@FDA application register on 2026-10-09 returned 1 application record(s) for this compound name (including NDA018469, marketed as BSS PLUS). Material supplied as a research chemical is not the subject of those applications and is not an FDA-approved product.
Sources
- PubChem Compound Summary for CID 124886, Glutathione. PubChem, National Library of Medicine (2026). pubchem:124886
- Drugs@FDA application register query for this compound, 1 application(s) returned: NDA018469. U.S. Food and Drug Administration, openFDA drugsfda endpoint (2026). fda:glutathione
- Glutathione. Annual review of biochemistry (1983). pmid:6137189
- Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free radical biology & medicine (2001). pmid:11368918
- Improved method for the determination of blood glutathione. The Journal of laboratory and clinical medicine (1963). pmid:13967893
- Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: applications to mammalian blood and other tissues. Analytical biochemistry (1969). pmid:4388022
- A fluorometric method for determination of oxidized and reduced glutathione in tissues. Analytical biochemistry (1976). pmid:962076
- Determination of glutathione and glutathione disulfide using glutathione reductase and 2-vinylpyridine. Analytical biochemistry (1980). pmid:7416462
- Glutathione S-transferases. The first enzymatic step in mercapturic acid formation. The Journal of biological chemistry (1974). pmid:4436300
- Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase. The Journal of laboratory and clinical medicine (1967). pmid:6066618
- Assays of glutathione peroxidase. Methods in enzymology (1984). pmid:6727659
- Selenium: biochemical role as a component of glutathione peroxidase. Science (New York, N.Y.) (1973). pmid:4686466
- Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene (1988). pmid:3047011
On each stated value was matched to the record cited for it. That is record matching, not an appraisal of the research. Compiled and checked by: Peptide Monographs editorial desk. No qualified clinical reviewer.