The short version of glutathione fits in a sentence. The long version — which is the one that helps — is below.
Reviewed 2026-08-01. Anything still debated is marked as such rather than presented as settled.
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.
Glutathione supports detoxification by conjugating reactive electrophiles through glutathione S-transferases. The resulting conjugates are processed and exported, often after further metabolism. It also stores cysteine, transports amino acids across membranes through the gamma-glutamyl cycle, and assists in the maturation of iron-sulfur clusters and some prostaglandins. In plants, animals, and many microbes, the molecule appears in similar roles, but concentrations vary enormously between tissues. Liver, kidney, and red blood cells tend to contain high amounts, while blood plasma contains much less.
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.
| Property | Value | Notes |
|---|---|---|
| Chemical formula | C10H17N3O6S | Refers to the reduced form |
| Molar mass | 307.32 g/mol | Calculated for the neutral molecule |
| Appearance | White crystalline powder | Often hygroscopic; protect from moisture |
| Water solubility | Soluble in water | Reported values vary with purity and form |
| Alternative names | GSH, reduced glutathione | GSH specifies the thiol form |
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.
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 functions in redox balance, detoxification, and sulfur amino acid storage. It participates in reactions that help maintain ascorbate and protein thiol status. The molecule serves as a cofactor for several enzymes, including glutathione peroxidases and glutathione S-transferases. These enzymes reduce peroxides and conjugate electrophiles, respectively. Glutathione also contributes to the metabolism of xenobiotics and to the transport of cysteine between tissues. How interorgan transport and tissue-specific regulation shape whole-body pools remains an active area of study.
Glutathione is a tripeptide composed of glutamate, cysteine, and glycine. Its cysteine residue carries a thiol group, which allows the molecule to participate in reduction and oxidation reactions. The compound exists in most living cells, where the reduced form, often abbreviated GSH, is usually more abundant than the oxidized disulfide form, GSSG. Intracellular concentrations are commonly in the millimolar range, while extracellular concentrations are much lower. This uneven distribution supports its role as a major cellular redox buffer.
Cells synthesize glutathione through two ATP-dependent enzymatic steps. The first step combines glutamate and cysteine to form gamma-glutamylcysteine, catalyzed by glutamate-cysteine ligase. The second step adds glycine, producing the complete tripeptide, catalyzed by glutathione synthetase. Glutathione itself can inhibit the first enzyme, providing negative feedback when levels are high. Because cysteine is often limiting, its availability influences how quickly the pathway proceeds. These reactions occur in the cytosol, and the resulting glutathione can be distributed to other compartments.
== External links == Media related to Protons at Wikimedia Commons Particle Data Group at LBL Large Hadron Collider Eaves, Laurence; Copeland, Ed; Padilla, Antonio (Tony) (2010). "The shrinking proton". Sixty Symbols. Brady Haran for the University of Nottingham. MIT proton visualization project: Inside the Proton, the 'Most Complicated Thing You Could Possibly Imagine', Quanta Magazine, Oct 19 2022 Visualizing the Proton, Arts at MIT, 2022
=== Awards === Half-Life: Alyx won "Game of the Year" at the 2020 VR Awards. At the Game Awards 2020, it was nominated for "Best Game Direction", "Best Audio Design" and "Best Action", and won for "Best VR/AR". At the 17th British Academy Games Awards, it was nominated for "Best Game", "Game Direction", "Audio Achievement" and "Artistic Achievement". At the 24th Annual D.I.C.E. Awards, it was nominated for "Action Game of the Year", "Outstanding Achievement in Game Direction", and "Outstanding Achievement in Game Design", and won for "Immersive Reality Technical Achievement" and "Immersive Reality Game of the Year".
Pre-existing acute or chronic liver dysfunction or family history of severe liver inflammation (hepatitis), particularly medicine related. Pregnancy 11% risk of birth defects and 30-40% risk of neuro-developmental disabilities which can be permanent Known hypersensitivity to valproate or any of the ingredients used in the preparation Urea cycle disorders Hepatic porphyria Hepatotoxicity Mitochondrial disease Pancreatitis Porphyria
Sources: en.wikipedia.org
Lemonhead is an American brand of candy that was first introduced in 1962 and is produced by the Ferrara Candy Company. Lemonheads are a round, lemon flavored candy consisting of a sweet coating, a soft, sour shell, and a hard candy core. Inspiration for the Lemonhead name came from Salvatore Ferrara seeing his grandson, Salvatore II, after delivery. Salvatore II was a forceps baby and he noted that his new grandson's head was lemon shaped. The candy was born out of the same cold panned process as the company's Red Hots in 1962. In this process, layer after layer of sugar and flavor are added until the candy reaches the desired shape and size. They are most commonly sold in their standard 1 centimeter size, but they are also produced in a single-sale 3 cm version. Lemonhead candies are gluten and fat-free. Ferrara now makes 500 million Lemonheads per year. Some time between the 1980s and late 1990s, Ferrara Pan brought all of their fruit flavored candies under a consistent naming convention: Lemonheads, Grapeheads (formerly Alexander the Grape), Cherryheads (formerly Cherry Chan/Cherry Clan) and Appleheads (formerly Johnny Apple Treats). Today, only the standard Lemonhead variety remains.
== Pathophysiological implications == In lean subjects it is significantly higher than in a population with obese persons. In several populations, SPINA-GR correlated with the area under the glucose curve and 2-hour concentrations of glucose, insulin and proinsulin in oral glucose tolerance testing, concentrations of free fatty acids, ghrelin and adiponectin, and the HbA1c fraction. SPINA-GR declines with increasing adherence to mediterranean diet, which may be explained by increased use of other macronutrients for energy production. In mice, SPINA-GR is reduced after they were fed a high-fat diet for one and three weeks. In hidradenitis suppurativa, an inflammatory skin disease, SPINA-GR is reduced. If this state is uncompensated by increased beta-cell function the static disposition index (SPINA-DI) is reduced, resulting in the onset of diabetes mellitus.
==== Cell division ==== In the final stages of cell division, many cells form a ring of actin at the cell's midpoint. This ring, aptly called the "contractile ring", uses a similar mechanism as muscle fibers where myosin II pulls along the actin ring, causing it to contract. This contraction cleaves the parent cell into two, completing cytokinesis. The contractile ring is composed of actin, myosin, anillin, and α-actinin. In the fission yeast Schizosaccharomyces pombe, actin is actively formed in the constricting ring with the participation of Arp3, the formin Cdc12, profilin, and WASp, along with preformed microfilaments. Once the ring has been constructed the structure is maintained by a continual assembly and disassembly that, aided by the Arp2/3 complex and formins, is key to one of the central processes of cytokinesis.
Sources: en.wikipedia.org
== Adverse effects == The most common side effects (seen in more than 1% of patients) are upper abdominal (belly) pain, diarrhoea, dry mouth, and nausea or vomiting. Allergic reactions of the skin like itching, rashes, hives and angiooedema are rare. The same is true for anaphylactic shock and convulsions.
=== Stability of naturally occurring nuclides === Most naturally occurring nuclides on earth are beta stable. Nuclides that are not beta stable have half-lives ranging from under a second to periods of time significantly greater than the age of the universe. One common example of a long-lived isotope is the odd-proton odd-neutron nuclide 4019K, which undergoes all three types of beta decay (β−, β+ and electron capture) with a half-life of 1.248×109 years.
I don't think there was anything else like it at the time. Before TGI Fridays, four single twenty-five-year-old girls were not going out on Friday nights, in public and with each other, to have a good time. They went to people's apartments for cocktail parties or they might go to a real restaurant for a date or for somebody's birthday, but they weren't going out with each other to a bar for a casual dinner and drinks because there was no such place for them to go. TGI Fridays was one of the first to use promotions such as ladies' night, and Stillman achieved his hopes of meeting women; "Have you seen the movie Cocktail? Tom Cruise played me!...Why do girls want to date the bartender? To this day, I'm not sure that I get it." He and the restaurant benefited from its location—according to Stillman, 480 stewardesses lived in the apartment building next door—and received publicity in national magazines. TGI Fridays became so popular that it had to install ropes to create an area for those waiting in line, also unusual at the time for a restaurant. A competitor, Maxwell's Plum, opened across the street, and others soon followed. With fellow Bucknell University graduate Ben Benson, Stillman opened other restaurants, including Tuesday's, Thursday's, Wednesday's, and Ice Cream Sunday's. Franchising of TGI Fridays began two years after the Manhattan location opened, in a since-closed location in Memphis, Tennessee's Overton Square district. In 1971, Daniel R. Scoggin acquired the rights to eight major Midwest cities. In 1972, he opened with the first of a new prototype in Dallas.
Clerodane acid A high-throughput library screen identified Clerodane acid, a natural product from Dodonaea viscosa, to be a selective activator of ERAP1 for small substrates and an inhibitor of peptide trimming. This compound was found active in blocking ERAP1-dependent antigen presentation (EC50 = 1μΜ) and to bind to the regulatory site of ERAP1 that normally accommodates C-termini of peptide substates. Clerodane acid was also found to induce strong immunopeptidome shifts in cancer cells.
Sources: en.wikipedia.org
It is a tripeptide of glutamate, cysteine, and glycine. The glutamate-cysteine bond is unusual because it forms through the gamma-carboxyl group.
It reflects the balance between oxidant exposure and antioxidant capacity. The ratio is not a direct clinical diagnosis and depends on the tissue and sample method.
No. It also participates in detoxification, amino acid transport, and protein modification. Its roles vary by cell type and compartment.
Glutathione is a tripeptide made from glutamate, cysteine, and glycine. Its cysteine residue provides a thiol group that is central to its redox activity. The glutamate-cysteine bond forms through the gamma-carboxyl group of glutamate.