This is a working overview of thiol group, written for readers who want more than a one-paragraph summary but less than a textbook.
Reviewed 2026-07-31. Anything still debated is marked as such rather than presented as settled.
Glutathione participates in detoxification reactions, amino acid transport, and the maintenance of protein thiols. It serves as a cofactor for several enzymes, including glutathione peroxidases and glutathione S-transferases. In research literature, altered glutathione status appears in studies of aging, infection, metabolic stress, and environmental exposure. Whether low glutathione is a cause, consequence, or marker of such conditions often remains unresolved. Direct measurement in blood or tissue provides a snapshot, but results depend on sample handling, timing, and the method used.
Glutathione is a small tripeptide made of glutamic acid, cysteine, and glycine. Its cysteine thiol group allows reversible oxidation and reduction, making it central to cellular redox chemistry. The reduced form, often abbreviated GSH, predominates inside most cells, while the oxidized disulfide form, GSSG, forms when two GSH molecules react. The ratio of GSH to GSSG is widely used as an indicator of oxidative stress in laboratory research, though it does not by itself diagnose a clinical condition.
Biosynthesis occurs in two ATP-dependent steps. The enzyme glutamate-cysteine ligase joins glutamate and cysteine, forming gamma-glutamylcysteine; glutathione synthetase then adds glycine to produce the complete tripeptide. Because the peptide bond from glutamate uses the gamma-carboxyl group, glutathione resists digestion by many ordinary peptidases. Tissues vary in synthesis capacity, and the liver generally contains high concentrations relative to many other organs. This uneven distribution contributes to organ-specific differences in redox buffering and affects how experimental results are interpreted across tissue types.
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 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.
| Property | Value | Notes |
|---|---|---|
| Molecular formula | C10H17N3O6S | Reduced glutathione (GSH); oxidized form differs by disulfide linkage. |
| Molar mass | 307.32 g/mol | Calculated for the reduced tripeptide. |
| Appearance | White to off-white crystalline powder | Typical laboratory reagent description. |
| Solubility | Soluble in water | Aqueous solutions are acidic; solubility depends on pH and salt form. |
| CAS Registry Number | 70-18-8 | Refers to reduced L-glutathione; oxidized form has a different number. |
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.
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.
Glutathione is a tripeptide composed of glutamate, cysteine, and glycine. It occurs in nearly all living cells, with highest concentrations in liver, kidney, and red blood cells, and exists in reduced (GSH) and oxidized disulfide (GSSG) forms. The cysteine thiol group enables reversible oxidation and reduction reactions. This property makes glutathione a central participant in cellular redox balance. The balance between these forms is often used as an indicator of oxidative stress.
Glutathione synthesis proceeds in two ATP-dependent steps catalyzed by glutamate-cysteine ligase and glutathione synthetase. The first step joins glutamate and cysteine to form gamma-glutamylcysteine and is generally rate-limiting. The second step adds glycine to complete the tripeptide. Cysteine availability, feedback inhibition by glutathione, and oxidative conditions influence flux through this pathway. The pathway is conserved across many organisms, and degradation by gamma-glutamyl transpeptidase and related peptidases recycles amino acids for new synthesis.
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.
Curium was first intentionally synthesized, isolated and identified in 1944, at University of California, Berkeley, by Glenn T. Seaborg, Ralph A. James, and Albert Ghiorso. In their experiments, they used a 60-inch (150 cm) cyclotron. Curium was chemically identified at the Metallurgical Laboratory (now Argonne National Laboratory), University of Chicago. It was the third transuranium element to be discovered even though it is the fourth in the series – the lighter element americium was still unknown. The sample was prepared as follows: first plutonium nitrate solution was coated on a platinum foil of ~0.5 cm2 area, the solution was evaporated and the residue was converted into plutonium(IV) oxide (PuO2) by annealing. Following cyclotron irradiation of the oxide, the coating was dissolved with nitric acid and then precipitated as the hydroxide using concentrated aqueous ammonia solution. The residue was dissolved in perchloric acid, and further separation was done by ion exchange to yield a certain isotope of curium. The separation of curium and americium was so painstaking that the Berkeley group initially called those elements pandemonium (from Greek for all demons or hell) and delirium (from Latin for madness). 242Cm was made in July–August 1944 by bombarding 239Pu with α-particles to produce curium with the release of a neutron:
== Deployment history == Georgia strongly supported the U.S.-led entrance of troops in Iraq for peacekeeping purposes and deployed troops to the country in August 2003. Georgia's military deployment was undertaken as part of broader efforts to bolster closer ties with the United States and NATO in the face of the continuing Russian threat. The United States provided military training programs—GTEP and GSSOP—for Georgian forces. There was no tangible domestic opposition to the Georgian involvement in Iraq. Georgia's initial deployment was a platoon of special forces and a medical team, a total of 70 personnel in 2003. The Georgian presence in Iraq increased to 300 personnel in 2004 and to 850 in 2005, and peaked at 2,300 soldiers in mid-2008. The largest contingents deployed were the 3rd Infantry Brigade (July 2007 – January 2008) and the 1st Infantry Brigade (January–August 2008). In addition to participation in Operation Iraqi Freedom, from 2005 to 2008 Georgia also contributed a battalion of approximately 550 troops to the United Nations Assistance Mission in Iraq, which was stationed in Baghdad within the "Green Zone". At first, the Georgian troops deployed for Operation Iraqi Freedom were stationed in Baghdad and provided general security measures. Beginning in 2007, the Georgians were deployed along the border with Iran, with their main base at Kut, and tasked to interdict smuggled weapons, goods, and drugs. The Georgian units worked primarily within the U.S. area of operations.
(2026) study the anatomy of ulna and femur or Sahelanthropus tchadensis, interpreted as indicative of presence of adaptations to bipedalism in spite of similarities in size and geometric morphometric shape to bones of chimpanzees. De Jager et al. (2026) study the frequency, position, and variability of cortical sulcal imprints in endocasts of extant chimpanzees and bonobos, providing a comparative resource for the studies of the brain evolution based on hominin fossils. Dunbar (2026) reevaluates data from the study of Deaner & Nunn (1999), finds evidence of changes in brain size following increases in body size in the evolution of primates but in a more complicated way that suggested by the original brain lag hypothesis, with an increase in body size followed by a progressively greater increase in brain size, and finds evidence of such evolution of brain and body size in hominins.
Crude oil varies greatly in appearance depending on its composition. It is usually black or dark brown (although it may be yellowish, reddish, or even greenish). In the reservoir it is usually found in association with natural gas (which being lighter forms a "gas cap" over the petroleum) and saline water (which being heavier than most forms of crude oil, generally sinks beneath it). Crude oil may also be found in a semi-solid form mixed with sand and water, as in the Athabasca oil sands in Canada, where it is usually referred to as crude bitumen. In Canada, bitumen is considered a sticky, black, tar-like form of crude oil which is so thick and heavy that it must be heated or diluted before it will flow. Venezuela also has large amounts of oil in the Orinoco oil sands, although the hydrocarbons trapped in them are less viscous than in Canada and are usually called extra heavy oil. Oil sands resources are called unconventional oil to distinguish them from oil which can be extracted using traditional oil well methods. Between them, Canada and Venezuela contain an estimated 3.6 trillion barrels (570×10^9 m3) of bitumen and extra heavy oil, about twice the volume of the world's reserves of conventional oil.
==== Member of the Order of the British Empire (MBE) ==== Civil Division Inspector Joe Arukai. For services to the Royal Papua New Guinea Constabulary. Sister Joseph Mary Cresp. For services to charity. Bamaga Morre Imari. For services to the community, public service and the government. Justin Hansu Kill. For services to broadcasting. Sally Mokis. For services to the Papua New Guinea Banking Corporation. Membup Paril. For public services and services to the community. Cecilia Ropa. For services to health and the community. Noki Timbil. For services to the community.
Sources: en.wikipedia.org
The fifth season had twelve roles receiving star billing, with eleven of them returning from the previous season, eight of which part of the original cast from the first season, and three new cast members being added. Kerry Washington continued to play her role as protagonist of the series, Olivia Pope, a former White House Director of Communications with her own crisis management firm. Darby Stanchfield played Abby Whelan, the White House Press Secretary, Katie Lowes portrayed Quinn Perkins, and Guillermo Diaz portrayed Huck, the troubled tech guy who works for Olivia. Cornelius Smith Jr. continued his role as activist Marcus Walker. after being upgraded to series regular. Jeff Perry continued to portray Cyrus Beene, chief of staff at the White House who was fired by Fitz but later rehired. Portia de Rossi played Elizabeth North, the new chief of staff at the White House, and later the chief of staff for the vice president. Joshua Malina played the role of David Rosen, former U.S. Attorney, now Attorney General. Bellamy Young continued to act as First Lady/Senator Melody "Mellie" Grant, who was kicked out of the White House by Fitz, and later joined the presidential campaign for president. Tony Goldwyn continued to portray President Fitzgerald "Fitz" Thomas Grant III. Scott Foley portrayed Jake Ballard a former B613 agent and later the head of the NSA. On May 14, 2015, after the fourth-season finale, it was announced that Portia de Rossi had been promoted to a series regular for the fifth season.
Sports tournaments in Jammu and Kashmir are organised by both the Indian army and police, as well as mainstream political parties and the All Parties Hurriyat Conference. Sportspersons who represent India in tournaments face stigmatisation from separatists. Jammu and Kashmir has 18 stadiums, 23 training centres, three indoor sports complexes and 42 government-maintained playing fields. Srinagar is home to the Sher-i-Kashmir Stadium, a stadium where international cricket matches have been played. The Maulana Azad Stadium in Jammu is one of the home venues for the Jammu and Kashmir cricket team. The Bakshi Stadium in Srinagar, named after Bakshi Ghulam Mohammad, hosts football matches. Institutions such as the Jawahar Institute of Mountaineering and Winter Sports provides mountaineering, skiing and adventure courses. The Royal Springs Golf Course, Srinagar, located on the banks of Dal lake, is considered one of the best golf courses in India. Jammu and Kashmir was also host to the first Khelo India Winter Games, held in 2020 in Gulmarg. Jammu and Kashmir came first with the most gold medals at 26, followed by the Indian Army team with 8 gold medals. The second edition of the winter games were also held in Gulmarg in 2021, with Jammu and Kashmir coming first again.
=== Laboratory uses === In the laboratory, this compound is used in complexometric titrations. A variant of NTA is used for protein isolation and purification in the His-tag method. The modified NTA is used to immobilize nickel on a solid support. This allows purification of proteins containing a tag consisting of six histidine residues at either terminus. The His-tag binds the metal of metal chelator complexes. Previously, iminodiacetic acid was used for that purpose. Now, nitrilotriacetic acid is more commonly used. For laboratory uses, Ernst Hochuli et al. (1987) coupled the NTA ligand and nickel ions to agarose beads. This Ni-NTA Agarose is the most used tool to purify His-tagged proteins via affinity chromatography.
Russell indexes are a family of global stock market indices from FTSE Russell that allow investors to track the performance of distinct market segments worldwide. Many investors use mutual funds or exchange-traded funds based on the FTSE Russell Indexes as a way of gaining exposure to certain portions of the U.S. stock market. Additionally, many investment managers use the Russell Indexes as benchmarks to measure their own performance. Russell's index design has led to more assets benchmarked to its U.S. index family than all other U.S. equity indexes combined. The best-known index of the series is the Russell 2000, which tracks US small-cap stocks and is made up of the bottom 2,000 stocks in the Russell 3000 index.
Sources: en.wikipedia.org
Long term neuropsychiatric difficulties are increasingly recognized (49 studies so far, especially obsessive-compulsive disorder but also attention-deficit hyperactivity disorder, affective disorders, tic disorders, executive function disturbances, psychotic features, and language impairment). Heart involvement improves in about a third of cases (whether silent or not).
== AFL career == Monfries was drafted by the Bombers with selection 14 in the 2004 AFL draft. He played football for Walkerville Junior Football Club before moving to Melbourne. He made his debut in Round 1, 2005 against Melbourne, which saw him become the 200th player to have played under coach Kevin Sheedy. Monfries maintained his position in the senior side until round 4, but was dropped for the Anzac Day clash in round 5, against Collingwood and did not play at senior level again until round 12. In round 13 against St Kilda, he kicked two goals and, alongside other young Bombers, played a role in a fifteen-point win. He then went on to play every game for the remainder of the season. In 2006, his second season, Monfries played 21 games, missing only one game due to a minor calf strain. In 2007, Monfries played 20 out of 22 games, omitted on form for two weeks at midseason. He was, however, named as an emergency for both matches and quickly returned to the team due to pressures caused by injuries and suspensions to other key players. In 2009, Monfries became a key player within the Essendon Football Club. He defined his role further as a key position forward and finished second in the club's goalkicking after Matthew Lloyd. On 5 October 2012, Angus told Essendon that he will be leaving and be signing a new four-year deal with Port Adelaide. On 8 October 2012, Essendon announced that Monfries would be traded to Port Adelaide for pick 48. He made his debut for Port Adelaide in round 1, 2013, against Melbourne.
Swiss chemist Albert Hofmann first synthesized LSD in 1938 and discovered its potent psychedelic effects in 1943 after accidental ingestion. It became widely studied in the 1950s and 1960s. The drug was initially explored for psychiatric use due to its structural similarity to serotonin and safety profile. It was used experimentally in psychiatry for treating alcoholism and schizophrenia. By the mid-1960s, LSD became central to the youth counterculture in places like San Francisco and London, influencing art, music, and social movements through events like Acid Tests and figures such as Timothy Leary, Owsley Stanley and Michael Hollingshead. Its psychedelic effects inspired distinct visual art styles and musical innovations, and caused a lasting cultural impact. However, its association with the counterculture movement of the 1960s led to its classification as a Schedule I drug in the United States in 1970. It was also listed as a Schedule I controlled substance by the United Nations in 1971 and remains without approved medical uses. Despite its legal restrictions, LSD remains influential in scientific and cultural contexts. Research on LSD declined due to cultural controversies by the 1960s, but has resurged since 2009. In 2024, the United States Food and Drug Administration designated LSD (code name MM120 or DT120) as a breakthrough therapy for generalized anxiety disorder. As of 2017, about 10% of people in the United States had used LSD at some point, with 0.7% having used it in the past year.
Sources: en.wikipedia.org
GSH is the reduced form of glutathione, with a free thiol group on cysteine. GSSG is the oxidized disulfide form, created when two GSH molecules become linked. The two forms exist together, and their balance is often reported as the GSH/GSSG ratio in laboratory studies.
Glutathione is synthesized inside cells from amino acids rather than being classified as an essential dietary nutrient. Dietary sources can provide glutathione or its precursors, but digestion and absorption alter what reaches tissues. Research continues on how dietary intake relates to cellular glutathione levels.
The liver has high glutathione concentrations and uses the compound in conjugation and antioxidant reactions. These reactions are relevant to the processing of drugs, pollutants, and normal metabolic byproducts. Studies often examine liver glutathione as a marker of oxidative stress or detoxification capacity.
It is a tripeptide of glutamate, cysteine, and glycine. The glutamate-cysteine bond is unusual because it forms through the gamma-carboxyl group.