A practical reference on thiol group: what it is, how it behaves, what the literature reports, and where the honest uncertainties sit.
Reviewed 2026-04-13. Anything still debated is marked as such rather than presented as settled.
Glutathione is a tripeptide composed of glutamate, cysteine, and glycine. It contains an unusual gamma-glutamyl bond between glutamate and cysteine, which resists cleavage by many peptidases. The reduced form, GSH, carries a thiol group on cysteine and is the dominant intracellular form in most cells. Its structure allows it to participate in redox reactions and to serve as a sulfur donor. The oxidized form, GSSG, consists of two GSH molecules joined by a disulfide bond.
In cells, glutathione helps maintain the reducing environment of the cytosol and supports enzymes that counteract reactive oxygen species. It acts as a cofactor for glutathione peroxidases, which reduce hydrogen peroxide and lipid peroxides, and for glutathione S-transferases, which conjugate electrophiles. The ratio of GSH to GSSG is often used as an indicator of oxidative stress, although the ratio can vary by compartment and cell type. Glutathione also stores cysteine, an amino acid that can be limiting for protein synthesis and antioxidant defense.
Synthesis occurs in two ATP-dependent steps. The enzyme glutamate-cysteine ligase joins glutamate and cysteine to form gamma-glutamylcysteine, and glutathione synthetase adds glycine. The first step is rate-limiting and is influenced by cysteine availability and feedback inhibition by GSH. Breakdown involves gamma-glutamyl transferase and subsequent peptidases, which release constituent amino acids for reuse. Because turnover differs among tissues, measurements from blood, plasma, and tissues are not directly interchangeable. Research continues to clarify how compartment-specific pools are regulated in health and disease.
Glutathione is a small tripeptide built from glutamic acid, cysteine, and glycine. Its peptide bond between glutamate and cysteine involves the gamma-carboxyl group rather than the usual alpha-carboxyl group. This structure gives the molecule a reactive thiol on the cysteine residue. The reduced form, often abbreviated GSH, is the predominant intracellular species in many cell types. Because the thiol can donate electrons, glutathione participates in redox chemistry and in the conjugation of reactive molecules.
Cells synthesize glutathione through two ATP-dependent steps: glutamate-cysteine ligase joins glutamate and cysteine, and glutathione synthetase adds glycine to form the complete tripeptide. Breakdown occurs through gamma-glutamyl transpeptidase and subsequent peptidase reactions, forming the gamma-glutamyl cycle. Within cells, glutathione also forms a disulfide-linked dimer called GSSG when two GSH molecules react. The balance between GSH and GSSG is widely used as an indicator of oxidative conditions, although the ratio can vary by compartment and tissue.
Glutathione supports several cellular processes beyond direct antioxidant action. It serves as a cofactor for glutathione peroxidase and glutathione S-transferase enzymes, which reduce peroxides and conjugate electrophiles, respectively. The molecule also acts as a reservoir of cysteine, an amino acid that can limit protein synthesis and redox signaling. In human nutrition, oral glutathione is sold as a supplement, but how much intact glutathione reaches tissues after ingestion remains an active research question. Clinical claims about supplementation are not uniformly supported by controlled trials.
| Property | Value | Notes |
|---|---|---|
| Chemical formula | C10H17N3O6S | For reduced glutathione; the oxidized dimer has two sulfur atoms. |
| Molar mass | 307.32 g/mol | Calculated for the reduced form. |
| Appearance | White to off-white crystalline powder | Typical for solid reagent; solutions are usually colorless. |
| Solubility | Freely soluble in water | Poorly soluble in nonpolar organic solvents. |
| Typical storage | -20 °C, desiccated, protected from light | Limits oxidation, moisture uptake, and degradation. |
Glutathione is a tripeptide composed of glutamate, cysteine, and glycine. The peptide bond between glutamate and cysteine uses the gamma-carboxyl group of glutamate rather than the alpha-carboxyl group. This unusual linkage protects the molecule from many common peptidases. The cysteine side chain carries a thiol group that can undergo reversible oxidation. Because of this thiol, glutathione participates in redox reactions and helps maintain the reducing environment inside most cells in living systems.
In cells, glutathione exists mainly in a reduced form called GSH. When two GSH molecules react, they form oxidized glutathione, or GSSG, which contains a disulfide bond. The ratio of GSH to GSSG is often used as an indicator of oxidative stress. Enzymes such as glutathione peroxidase and glutathione reductase help cycle the molecule between these two states. This cycling supports antioxidant defense, detoxification of reactive molecules, and regulation of certain signaling pathways.
Glutathione is a small tripeptide built from glutamate, cysteine, and glycine. The peptide bond between glutamate and cysteine uses the gamma-carboxyl group, a linkage that resists ordinary peptidases. Cells make it in two ATP-dependent steps: gamma-glutamylcysteine synthetase joins glutamate and cysteine, then glutathione synthetase adds glycine. The pathway is feedback-inhibited by glutathione itself, so intracellular levels tend to stay within a narrow range. Because cysteine is often limiting, sulfur amino acid supply influences how much glutathione a cell can produce.
In its reduced form, glutathione carries a sulfhydryl group that can donate electrons. This property lets it act as a major cellular antioxidant and redox buffer. Glutathione peroxidase uses it to reduce hydrogen peroxide and lipid peroxides, while glutathione reductase regenerates the reduced form using NADPH. The ratio of reduced glutathione to glutathione disulfide is widely used as an indicator of oxidative stress, though the ratio changes with compartment, cell type, and sample handling. Oxidized glutathione can also form mixed disulfides with proteins, affecting their activity.
=== Anti-microbial function === Being highly motile, neutrophils quickly congregate at a focus of infection, attracted by cytokines expressed by activated endothelium, mast cells, and macrophages. Neutrophils express and release cytokines, which in turn amplify inflammatory reactions by several other cell types. In addition to recruiting and activating other cells of the immune system, neutrophils play a key role in the front-line defense against invading pathogens, and contain a broad range of proteins. Neutrophils have three methods for directly attacking microorganisms: phagocytosis (ingestion), degranulation (release of soluble anti-microbials), and generation of neutrophil extracellular traps (NETs).
== See also == Digital mammography: use of a computer to produce images of the breast Global radiology: improving access to radiology resources in poor and developing countries Medical radiography: the use of ionizing electromagnetic radiation, such as X-rays, in medicine Radiation protection: the science of preventing people and the environment from suffering harmful effects from ionizing radiation Radiologists Without Borders Radiosensitivity: measure of the susceptibility of organic tissues to the harmful effects of radiation X-ray image intensifier: equipment that uses X-rays to produce an image feed displayed on a TV screen International Day of Radiology: an awareness day for medical imaging Electrogram
Diclazepam (Ro5-3448), also known as chlorodiazepam and 2'-chloro-diazepam, is a benzodiazepine and functional analog of diazepam. It was first synthesized by Leo Sternbach and his team at Hoffman-La Roche in 1960. It is not currently approved for use as a medication, but rather sold as an unscheduled substance. Efficacy and safety have not been tested in humans. In animal models, its effects are similar to diazepam, possessing long-acting anxiolytic, anticonvulsant, hypnotic, sedative, skeletal muscle relaxant, and amnestic properties.
Sources: en.wikipedia.org
Miriam Gross, Lady Owen; literary editor and writer; literary editor of The Observer, arts editor of The Daily Telegraph, literary editor of The Sunday Telegraph, senior editor (and co-founder) of Standpoint; edited Channel Four's Book Choice; at The Observer, she conducted a series of interviews, with, among others, the poet Philip Larkin, playwright Harold Pinter, thriller writer John le Carré, painters Francis Bacon and David Hockney, Nobel Prize-winning Russian poet Joseph Brodsky, novelist Anthony Powell, philosopher and historian Sir Isaiah Berlin, philosopher A.J. Ayer, and Stalin's daughter Svetlana Stalin; has written for the Financial Times; has also served as judge on the Booker prize and on George Orwell memorial prize. Susanna Gross, literary editor of The Mail on Sunday since 1999 and columnist for The Spectator; previously worked as an editor at the Daily Mail, was features editor of Harper's Bazaar, and was deputy editor of The Week; daughter of literary critic and writer John Gross and literary editor Miriam Gross, and the granddaughter of humanitarian Kurt May, she is married to novelist and critic John Preston; brother Tom Gross is a journalist and international affairs commentator, specialising in the Middle East; stepdaughter of Sir Geoffrey Owen.
Rafflesia hasseltii is a parasitic plant species of the genus Rafflesia and the family Rafflesiaceae which is hosted by certain Tetrastigma species. It is native to Sumatra and Peninsular Malaysia. R. hasseltii has by far the widest variation in form, color and pattern of any of the rafflesias.
== History == Yo-Chi's first store opened in September 2012, in the inner Melbourne suburb of Balaclava. In 2018, Yo-Chi was sold to chef and television personality George Calombaris, under his company MAdE Establishment Group. In 2020, following Calombaris' establishment going into voluntary administration, where Yo-Chi was the only part to survive, it was then sold to Oliver & Riley Allis, sons of Boost Juice founder Janine Allis. The brothers were just 23 and 21 years old respectively at the time of the sale. There were only four locations at the time. Under the Allis family, the number of stores have rapidly increased, opening their 30th store in June 2024, having 43 locations by March 2025, 53 by June 2025, 56 by August 2025, and opening their 70th store in March 2026. In August 2025, Yo-Chi began their international expansion, opening a store in Singapore and their first UK store in London's Notting Hill in 2026.
Sources: en.wikipedia.org
=== Glandular tissue === Glandular tissue is the type of epithelium that forms the glands from the infolding of epithelium and subsequent growth in the underlying connective tissue. They may be specialized columnar or cuboidal tissues consisting of goblet cells, which secrete mucus. Several glands contain myoepithelial cells that help in the contraction needed for secretion. There are two major classifications of glands: endocrine glands and exocrine glands:
254Es was used as the calibration marker in the chemical analysis spectrometer ("alpha-scattering surface analyzer") of the Surveyor 5 lunar probe. The large mass of this isotope reduced the spectral overlap between signals from the marker and the studied lighter elements of the lunar surface.
Two somewhat longer chapters in the book deviate slightly from the rest of the text because they do not contain any image analysis but instead focus on individual persons. Particularly noteworthy is the last part of the second chapter, which movingly describes the life story and the mission of Father Paolo Dall'Oglio, who for Kermani embodies everything he admires about Christianity: a form of unconditional love for one's neighbor that, especially in monks and nuns, goes beyond what a person can achieve without God. Kermani vividly describes the great love for Islam that characterizes Father Paolo and the Mar Musa monastery Paolo founded in Syria, which Kermani characterizes as a place of coexistence between religions. For Father Paolo, his conversion to Islam was not an act of benevolence but rather one that enriched his own life and faith; he is a monk, a disciple of Jesus, who is in love with Islam – as Kermani puts it. Kermani clearly sees this as a model for interfaith dialogue and Christian-Muslim rapprochement. By kidnapping the priest Father Paolo, who loves Islam like no other, the Islamic State has attempted to force Christians to fear Islam as an enemy. Kermani counters this attempt at intimidation with a declaration of his own love for Christianity, responding to Father Paolo and demonstrating how love can be used to counter violence. Kermani also repeatedly explains in his book how he has learned from Christianity—for example, in terms of remembering the suffering and death of others.
Sources: en.wikipedia.org
GSH is the reduced form with a free thiol group, while GSSG is the oxidized disulfide-linked dimer. Most assays distinguish the two because their balance reflects redox conditions. The names are not interchangeable.
It is synthesized in the body from amino acids, so it is not classified as an essential dietary nutrient for most people. Dietary and supplemental forms are studied for their effects on tissue levels and health markers. Evidence varies by population and outcome.
The phrase highlights its high intracellular concentration and its role in several antioxidant and detoxification reactions. It is not the only antioxidant, and the term can oversimplify its functions. Scientific descriptions usually specify the pathway or enzyme involved.
It is a tripeptide of glutamic acid, cysteine, and glycine. The linkage between glutamate and cysteine uses the gamma-carboxyl group, which is unusual for peptides.