This is a working overview of thiol group, written for readers who want more than a one-paragraph summary but less than a textbook.
This page was last updated on 2025-11-17 and is reviewed periodically as new material appears.
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 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.
Biosynthesis proceeds in two ATP-dependent steps. First, glutamate-cysteine ligase joins glutamate and cysteine. Second, glutathione synthetase adds glycine to the intermediate. The pathway is regulated by cysteine availability, enzyme expression, and feedback inhibition by glutathione itself. Liver tissue has a particularly high capacity for synthesis and export. Because the molecule is made inside cells, circulating glutathione reflects a balance of release, uptake, and breakdown rather than simple dietary supply.
Functionally, glutathione supports redox balance by donating electrons and becoming oxidized. It also serves as a cofactor for enzymes such as glutathione peroxidases and glutathione S-transferases. These enzymes participate in peroxide reduction and in conjugation reactions that help process reactive molecules. Separate from antioxidant roles, glutathione can modify protein cysteines through S-glutathionylation, influencing enzyme activity and signaling. Research continues to examine how these chemical roles translate into whole-organism effects.
Glutathione is a tripeptide composed of glutamate, cysteine, and glycine. Its glutamate-cysteine linkage uses the gamma-carboxyl group of glutamate, a feature that resists standard peptidases. The cysteine residue provides a thiol group, which gives the molecule its reducing character. In cells, glutathione is often the most abundant small-molecule thiol, with concentrations varying widely by tissue and compartment. It exists mainly in a reduced form called GSH, while oxidation produces a disulfide-linked dimer called GSSG.
| 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. |
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.
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 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.
{\displaystyle \Delta _{^{12}CH_{2}D_{2}}={\left({\frac {0.183798}{T}}\right)}-{\left({\frac {785.483}{T^{2}}}\right)}+\left({\frac {1056280.0}{T^{3}}}\right)+\left({\frac {9.37307\times 10^{7}}{T^{4}}}\right)-\left({\frac {8.919480\times 10^{10}}{T^{5}}}\right)+\left({\frac {9.901730\times 10^{12}}{T^{6}}}\right)}
== Legislative and regulatory matters == Traceability of food is legally required in the European Union (Regulation 178/2002) with dedicated initiatives in EU countries and the UK and Northern Ireland. In the EU, under the renewed Sustainable Product Policy Initiative, the inclusion of a Digital Product Passport has been proposed. The EU sustainable product policy was renewed in function of the European Green Deal and the new Circular Economy Action Plan. and revises the Ecodesign Directive. As such, similarly to material passports, it intents to assist the circular economy. In the United States, various government agencies have oversight or regulatory control over different aspects of fresh fruit and produce production, processing and distribution. These include the U.S. Department of Agriculture, the U.S. Food and Drug Administration (FDA) and the Centers for Disease Control. Some groups have pushed for a single food-safety agency, on-farm improvements and improved reporting and surveillance of foodborne illness outbreaks. The draft Food Safety Enhancement Act of 2009 was introduced May 27, 2009, in the U.S. House of Representatives. It would expand FDA authority, require registration of food manufacturers and processors, regulate crop cultivation and harvesting and other measures. After committee hearings and extensive amendment, the bill (HR2749) passed the House on July 30, 2009. HR2749 does not specifically endorse the PTI, or prescribe a traceability method or methodology, but instead Section 107 calls for regulations establishing a tracing system that includes:
After the jerky is dried to the proper moisture content to prevent spoilage, it is cooled and then packaged in (often resealable) plastic bags, either nitrogen gas flushed or vacuumed packed. The sealed packages usually contain small pouches of oxygen absorber to avoid fat oxidation. These small packets are filled with iron particles, which react with oxygen, removing the oxygen from the sealed jerky package and from an opened and resealed unfinished packet. Because of the necessary low fat and moisture content, jerky is high in protein. For example, a 30 g (about 1 oz) portion of lean meat contains about 7 g of protein. By removing 15 g of water from the meat, the protein ratio is doubled to nearly 15 g of protein per 30 g portion. In some low moisture varieties, a 30 g serving will contain 21 g of protein, and only one g of fat. The price per unit weight of this type of jerky is higher than less-dried forms, as it takes 90 g of 99% lean meat to generate 30 g of jerky. Unpackaged fresh jerky made from sliced, whole-muscle meat has been available in specialty stores in such places as Hong Kong at least since the 1970s. The products are purchased in kilograms, and customers choose from 10 to 20 types of meat used to make the product. Some are sold in strands instead of slices. Compared to the sealed packaged versions, unpackaged jerky has a relatively short shelf life. This type of jerky has also become very popular in convenience stores in the United States, where it is usually sold in clear plastic containers under the name "slab" jerky.
is the plate or tray efficiency. So-called bubble-cap or valve-cap trays are examples of the vapor and liquid contact devices used in industrial distillation columns. Another example of vapor and liquid contact devices are the spikes in laboratory Vigreux fractionating columns. The trays or plates used in industrial distillation columns are fabricated of circular steel plates and usually installed inside the column at intervals of about 60 to 75 cm (24 to 30 inches) up the height of the column. That spacing is chosen primarily for ease of installation and ease of access for future repair or maintenance.
Sources: en.wikipedia.org
== Society and culture == Benzocaine is found, particularly in Britain in the 2010s, as an additive in street cocaine and also as a bulking agent in "legal highs". Benzocaine gives a numbing effect similar to cocaine and as a bulking and binding agent it can not be detected once mixed. It is the most popular cutting agent worldwide.
=== Carnivores === Male felids are able to urinate backwards by curving the tip of the glans penis backward. In cats, the glans penis is covered with spines. Penile spines also occur on the glans of male and female spotted hyenas. In male dogs the glans penis is smooth and consists of two parts called the bulbus glandis and pars longa glandis. The glans of a fossa's penis extends about halfway down the shaft and is spiny except at the tip. In comparison, the glans of felids is short and spiny, while that of viverrids is smooth and long.
== Medical uses == The primary measure of efficacy in the clinical trials is three or more spontaneous complete bowel movements per week; a secondary measure is an increase of at least one complete spontaneous bowel movement per week. Further measures are improvements in PAC-QOL (a quality of life measure) and PAC-SYM (a range of stool, abdominal, and rectal symptoms associated with chronic constipation). Infrequent bowel movements, bloating, straining, abdominal pain, and defecation urge with inability to evacuate can be severe symptoms, significantly affecting quality of life. In three large clinical trials, 12 weeks of treatment with prucalopride 2 and 4 mg/day resulted in a significantly higher proportion of patients reaching the primary efficacy endpoint of an average of ≥3 spontaneous complete bowel movements than with placebo. There was also significantly improved bowel habit and associated symptoms, patient satisfaction with bowel habit and treatment, and HR-QOL in patients with severe chronic constipation, including those who did not experience adequate relief with prior therapies (>80% of the trial participants). The improvement in patient satisfaction with bowel habit and treatment was maintained during treatment for up to 24 months; prucalopride therapy was generally well tolerated. Small clinical trials suggested that prucalopride administration results in the 5-HT4 receptor agonism-associated memory enhancing in healthy participants improving their ability to recall and increasing neural activation in the hippocampus and functionally related areas.
In common with other nitriles, acetonitrile can be metabolised in microsomes, especially in the liver, to produce hydrogen cyanide, as was first shown by Pozzani et al. in 1959. The first step in this pathway is the oxidation of acetonitrile to glycolonitrile by an NADPH-dependent cytochrome P450 monooxygenase. The glycolonitrile then undergoes a spontaneous decomposition to give hydrogen cyanide and formaldehyde. Formaldehyde, a toxin and a carcinogen on its own, is further oxidized to formic acid, which is another source of toxicity. The metabolism of acetonitrile is much slower than that of other nitriles, which accounts for its relatively low toxicity. Hence, one hour after administration of a potentially lethal dose, the concentration of cyanide in the rat brain was 1/20 that for a propionitrile dose 60 times lower (see table). The relatively slow metabolism of acetonitrile to hydrogen cyanide allows more of the cyanide produced to be detoxified within the body to thiocyanate (the rhodanese pathway). It also allows more acetonitrile to be excreted unchanged before it is metabolised. The main pathways of excretion are by exhalation and in the urine.
Analysis of mitochondrial DNA by German herpetologist Wolfgang Wüster and colleagues in 2005 found the Papuan and nominate subspecies to be very similar genetically; however, their distinct coloration and limited sampling led Wüster to refrain from lumping the subspecies into a single taxon. Raymond Hoser described Oxyuranus scutellatus barringeri from a specimen collected from the Mitchell Plateau, however Wüster declared this a nomen nudum as the author did not explain how it was distinct. Hoser replied that it was distinct on the basis of DNA and distribution, and published it under a different subspecific name—O. scutellatus andrewwilsoni—in 2009, reporting it had a more rounded head and rougher neck scales than other subspecies of coastal taipan, and lacked a lighter colour on the snout. Kinghorn gave it the name "giant brown snake" in 1930, before Thomson introduced the term taipan in 1933. It is commonly called the coastal taipan, common taipan, or simply taipan. The New Guinea subspecies is known as the Papuan taipan. Local names in New Guinea include dirioro by the people of Parama village near the Fly River, and gobari near the Vailala River.
Sources: en.wikipedia.org
To visually identify legions, they also bore a specific emblem, a symbolic representation of the legion, frequently an animal or mythological figure, which appeared on the vexillum, a small rectangular flag that served as the legion's standard and carried both the emblem and name of the legion.
== Function == Citrulline is a metabolic intermediate within the urea cycle, which is the pathway by which mammals excrete ammonia by converting it into urea. Citrulline is also produced as a byproduct of the enzymatic production of nitric oxide from the amino acid arginine, catalyzed by nitric oxide synthase. In the yeast species Saccharomyces cerevisiae, citrulline is a metabolic intermediate in the latter, cytosolic half of the arginine biosynthesis pathway. Several proteins contain citrulline as a result of a post-translational modification. These citrulline residues are generated by a family of enzymes called peptidylarginine deiminases, which convert arginine into citrulline in a process called citrullination or deimination with the help of calcium ions. Proteins that normally contain citrulline residues include myelin basic protein, filaggrin, and several histone proteins, whereas other proteins, such as fibrin and vimentin are susceptible to citrullination during cell death and tissue inflammation. Circulating citrulline concentration is a biomarker of intestinal functionality.
Peyote was first described by Bernardino de Sahagún in 1560. It was first scientifically named as Peyotl zacatensis by Francisco Hernández in 1638. Botanical studies of peyote began in the 1840s and the drug was listed in the Mexican pharmacopeia. The first use of mescal buttons was published by John Raleigh Briggs in 1887. However, he took a very low dose of the drug, and in the modern literature, the symptoms he experienced have been attributed to a severe panic attack in response to the drug. In 1887, the German pharmacologist Louis Lewin received his first sample of the peyote cactus, found numerous new alkaloids and later published the first methodical analysis of it. The effects of mescaline in humans were first properly described by D. W. Prentiss and Francis P. Morgan in 1895. Mescaline was first isolated and identified in 1897 by the German chemist Arthur Heffter. He showed that mescaline was exclusively responsible for the psychoactive or hallucinogenic effects of peyote. However, other components of peyote, such as hordenine, pellotine, and anhalinine, are also active. Mescaline was first synthesized in 1919 by Ernst Späth. Three major books on mescaline and/or peyote were published in the mid-to-late 1920s.
The first MP, installed at Yale in 1963, operated consistently at 10–11 megavolts; a later installation at Strasbourg reached 18. At these energies, electron stripping becomes highly efficient. A uranium ion passing through the terminal can lose more than 20 electrons, enabling heavy-ion fusion experiments impossible with earlier machines. Advances in gamma-ray spectroscopy combined with MP tandems enabled precision measurements of nuclear structure. HVEC manufactured 10 MP units between 1965 and 1973 for institutions including the University of Minnesota, Chalk River, and the Max Planck Institute in Heidelberg. The XTU ("Holy Roman Emperor") was designed for superheavy element synthesis. Theoretical models predicted an "island of stability" beyond element 110 where nuclei would resist rapid decay. The XTU's 20-megavolt rating would accelerate uranium ions to nearly one billion electron volts—enough to overcome Coulomb barriers in heavy-element fusion. Two prototypes operated solely on a test basis at Burlington before the project was cancelled. One later sold to Italy's national laboratory at Legnaro in 1979.
== Discovery == The first long-acting (depot) injections were antipsychotics fluphenazine and haloperidol. The concept of a depot injection arose before 1950, and originally was used to describe antibiotic injections that lasted longer to allow for less frequent administration.
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.
Glutathione is a sulfur-containing tripeptide made from glutamate, cysteine, and glycine. It is found in most cells and participates in redox balance and detoxification reactions.