redox homeostasis raises a handful of sensible questions. This page answers them in order, starting with the fundamentals and moving to applications.
This page was last updated on 2025-11-11 and is reviewed periodically as new material appears.
Common analytical approaches include enzymatic recycling assays, high-performance liquid chromatography, and mass spectrometry. Enzymatic recycling measures total glutathione after converting GSSG back to GSH, while separation methods can quantify GSH and GSSG separately. Derivatization may be used to improve detection or stability during analysis. LC-MS/MS offers high specificity and can distinguish glutathione from related thiols and adducts. Each method has different sensitivity, throughput, and susceptibility to interference, so method selection depends on the study question and sample matrix.
For solid glutathione reagents, storage at low temperature and protection from moisture and light are typical precautions. Aqueous solutions can oxidize over time, and pH affects stability; alkaline conditions generally promote thiol oxidation. Some protocols prepare fresh solutions, while others use antioxidants or chelators to limit metal-catalyzed oxidation. Purity and counterion content can vary among commercial preparations, affecting concentration calculations. Certificates of analysis and validated assays help verify identity and purity.
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 present in most tissues, with especially high concentrations in the liver. It also serves as a cofactor for some enzymes and helps transport amino acids across cell membranes. In plants and microorganisms, glutathione contributes to stress responses and metal handling. The molecule is synthesized in two ATP-dependent steps, first producing gamma-glutamylcysteine and then adding glycine. Because cysteine availability often limits synthesis, dietary and metabolic factors can influence glutathione levels. Research continues to examine how these levels relate to health and disease.
| Property | Value | Notes |
|---|---|---|
| Typical analytical method | LC-MS/MS, HPLC, or enzymatic recycling | Choice depends on whether total, reduced, or oxidized glutathione is measured. |
| Sample stabilization | Acidification or thiol alkylation | Helps limit conversion of GSH to GSSG after collection. |
| Solution stability | Limited at room temperature | Oxidation and pH-dependent degradation can occur. |
| Storage of solid | -20 °C, desiccated, protected from light | Common for research reagents; follow supplier instructions. |
| Common interference | Other thiols and metal ions | Can affect separation or enzymatic detection. |
Glutathione is synthesized in two ATP-dependent steps. First, gamma-glutamylcysteine synthetase links glutamate and cysteine; second, glutathione synthetase adds glycine to form the complete tripeptide. The pathway is feedback-inhibited by GSH itself, which helps maintain steady intracellular levels. Tissues vary widely in glutathione content, with the liver typically containing the highest concentrations, followed by the kidneys, lungs, and erythrocytes. Because cysteine is often limiting, its availability influences synthesis rates, and regulation of this pathway varies by cell type.
Glutathione serves as a cofactor for several enzymes, including glutathione peroxidase and glutathione S-transferase. These enzymes help reduce hydrogen peroxide and lipid peroxides, and they conjugate reactive electrophiles for excretion. The molecule also acts as a reservoir for cysteine, an amino acid that is prone to oxidation. In addition, glutathione participates in the metabolism of nitric oxide, leukotrienes, and prostaglandins. Its roles extend to cell signaling, apoptosis, and the regulation of protein function through S-glutathionylation.
Glutathione is a tripeptide composed of glutamate, cysteine, and glycine, and it is the most abundant non-protein thiol in most living cells. The reduced form, GSH, carries a sulfhydryl group that can donate electrons, while the oxidized form, GSSG, forms when two GSH molecules link via a disulfide bond. The balance between these two forms helps define the cellular redox environment, and their ratio is often used as an indicator of oxidative stress. Because the sulfhydryl group is reactive, glutathione participates in many cellular processes, including detoxification and protein regulation.
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.
Conolidine is an indole alkaloid. Preliminary reports suggest that it could provide analgesic effects with few of the detrimental side-effects associated with opioid. Conolidine was first isolated in 2004 from the bark of the Tabernaemontana divaricata (crape jasmine) shrub which is used in traditional Chinese medicine. The first asymmetric total synthesis of conolidine was developed by Micalizio and coworkers in 2011. This synthetic route allows access to either enantiomer (mirror image) of conolidine via an early enzymatic resolution. Notably, evaluation of the synthetic material resulted in the discovery that both enantiomers of the synthetic compound show analgesic effects.
During 2020, as the COVID‑19 pandemic escalated globally and vaccine development intensified, the World Health Organization (WHO) COVAX facility adopted the motto "No one is safe unless everyone is safe" to emphasize the need for equitable vaccination. The facility set a goal of supplying COVID‑19 vaccines to nearly 100 low-to-middle income countries that could not afford them. COVAX sought to fundraise US$6.8 billion to purchase and deliver vaccines to participating countries in proportion to their populations. On 18 December 2020, the facility announced agreements with vaccine manufacturers to supply 1.3 billion doses for 92 low-middle income countries in the first half of 2021. Yet, by mid-December, some 16 countries representing only 14% of the world's population had preordered more than 10 billion vaccine doses or about 51% of the available world supply. Specifically, Canada, Australia, and Japan – having only 1% of the world's COVID‑19 cases – had collectively reserved some 1 billion vaccine doses, while the COVAX facility had reserved only a few hundred million doses. At the Group of Seven summit in June 2021, the United States promised to distribute 500 million vaccine doses internationally; this distribution began on 17 August. Preorders from rich countries were made during 2020 with 13 different vaccine manufacturers, whereas those for low-to-middle income countries were made primarily for the Oxford–AstraZeneca COVID-19 vaccine, which is lowest in cost and has no special refrigeration needs.
=== Cultivation === Royal jelly is harvested by stimulating colonies with movable frame hives to produce queen bees. Royal jelly is collected from each individual queen cell (honeycomb) when the queen larvae are about four days old. These are the only cells in which large amounts are deposited. This is because when royal jelly is fed to worker larvae, it is fed directly to them, and they consume it as it is produced, while the cells of queen larvae are "stocked" with royal jelly much faster than the larvae can consume it. Therefore, only in queen cells is the harvest of royal jelly practical. A well-managed hive during a season of 5–6 months can produce approximately 500 g (18 oz) of royal jelly. Since the product is perishable, producers must have immediate access to proper cold storage (e.g., a household refrigerator or freezer) in which the royal jelly is stored until it is sold or conveyed to a collection center. Sometimes honey or beeswax is added to the royal jelly, which is thought to aid its preservation. The Vegetarian Society considers royal jelly to be non-vegan.
Sources: en.wikipedia.org
== Discontinued operations == In 1998, Dairy Farm sold out its 49% interest in Nestlé Dairy Farm, set up in 1992 to develop dairy products factories throughout China, to Nestlé; on the merger of Kwik Save with Somerfield, Dairy Farm sold its 11% holding for US$290 million. Dairy Farm acquired 25% of the "No Frills" Kwik Save Group in 1987; Sold the 108-store Simago chain in Spain acquired in 1990. In March 2000, Dairy Farm sold its half share in DFI Géant, the Taiwan hypermarket opened in 1998 back to Casino, its joint venture partner. In 2001, the company sold the 287-store Franklins chain in Australia which it acquired in 1978. Its Hong Kong–based distribution business, Sims Trading, was sold to CITIC Pacific. In June 2002, the 61-store Woolworths chain in New Zealand acquired in 1990, was sold for US$337 million. In 2004, the Group's Hong Kong ice manufacturing business which began in 1918 was sold for US$107 million. In 2023, the Group's Malaysian food retailing business was sold to Macrovalue Sdn Bhd On 19 April 2024, DFI's subsidiary PT Hero Supermarket Tbk announced it would divest its supermarket businesses along with the rights to the Hero brand to PT Hero Retail Nusantara for 135 billion rupiahs. In 2025, DFI Retail Group in Singapore announced the sale of its food retail operations (Cold Storage, CS Fresh, Jasons Deli, and Giant) to Malaysian-based Macrovalue for S$125 million.
=== Narcolepsy === While MCH does promote sleep, there has been no research that links MCH to narcolepsy. Research has instead found that in individuals with narcolepsy there is a decrease in orexin neurons, which would promote wakefulness, while the number of MCH neurons do not vary from the average non-narcoleptic individual.
For the record robbery, he was sentenced to eight years in prison, but three weeks after the verdict, in July 1976, he fled again, this time by driving a Scania truck through three prison gates at Norrköping Prison. Together with a number of fellow prisoners, they fled to a waiting getaway car. On 31 July 1976, he was arrested in Halmstad. On 12 August 1976, Olofsson married Belgian national Marijke Demuynck in Kumla Prison. In 1979, while still in prison, Olofsson began studies in journalism at Stockholm University. He did an internship at the newspaper Arbetaren. During a leave on Midsummer's Eve in 1980, Olofsson got into a fight with fisherman Leif Sundin on Möja. The sentence was two and a half years for assault. His studies were interrupted by the verdict, but he eventually graduated in 1983. Olofsson was released in 1983; he then left Sweden with his wife and settled in her home country of Belgium. In November 1984, he was arrested in the port city of Blankenberge in Belgium, suspected of having tried to smuggle 25 kilograms of amphetamine into Sweden with the so-called Televerksligan ("Televerket Gang"). He was sentenced to ten years in prison for complicity in an aggravated felony drug offense.
=== Structural Biology and Protein Engineering === This program studies biomolecules using protein engineering and molecular biology techniques. Methodologies include X-ray crystallography and cryo-EM. Research includes protein structure determination and mass spectrometry methods.
Sources: en.wikipedia.org
== Books == Interstellar Grains (Chapman & Hall, London, 1967) Light Scattering Functions for Small Particles with Applications in Astronomy (Wiley, New York, 1973) Solid-State Astrophysics (ed. with D.J. Morgan) (D. Reidel, Boston, 1975) Interstellar Matter (with F.D. Khan & P.G. Mezger) (Swiss Society of Astronomy and Astrophysics, 1974) The Cosmic Laboratory (University College of Cardiff, 1975) Lifecloud: The Origin of Life in the Universe (with Fred Hoyle) (J.M. Dent, London, 1978) Diseases from Space (with Fred Hoyle) (J.M. Dent, London, 1979) Origin of Life (with Fred Hoyle) (University College Cardiff Press, 1979) Space Travellers: The Bringers of Life (with Fred Hoyle) (University College Cardiff Press, 1981) Evolution from Space (with Fred Hoyle) (J.M.
Whole lung lavage. this method involves repeatedly flushing the lungs with saline under intravenous anesthesia, together with mechanical ventilation, to remove the pathogenic factor Stopping further exposure to airborne silica, silica dust and other lung irritants, including tobacco smoking. Cough suppressants. Antibiotics for bacterial lung infection. Tuberculosis (TB) prophylaxis for those with positive tuberculin skin test or IGRA blood test. Prolonged anti-tuberculosis (multi-drug regimen) for those with active TB. Chest physiotherapy to help the bronchial drainage of mucus. Oxygen administration to treat hypoxemia, if present. Bronchodilators to facilitate breathing. Lung transplantation to replace the damaged lung tissue is the most effective treatment, but is associated with severe risks of its own from the lung transplant surgery as well as from consequences of long-term immunosuppression (e.g., opportunistic infections). For acute silicosis, bronchoalveolar lavage may alleviate symptoms, but does not decrease overall mortality. Preliminary work utilizing whole lung lavage for patients with artificial stone-associated silicosis has shown significant radiological improvement following the treatment.
== Function == This Non-receptor tyrosine-protein kinase plays an important role in the regulation of cell growth, differentiation, migration and immune response. CSK acts by suppressing the activity of the Src family of protein kinases by phosphorylation of Src family members at a conserved C-terminal tail site in Src. Upon phosphorylation by other kinases, Src-family members engage in intramolecular interactions between the phosphotyrosine tail and the SH2 domain that result in an inactive conformation. To inhibit SFKs, CSK is then recruited to the plasma membrane via binding to transmembrane proteins or adapter proteins located near the plasma membrane and ultimately suppresses signaling through various surface receptors, including T-cell receptor (TCR) and B-cell receptor (BCR) by phosphorylating and maintaining inactive several effector molecules.
reducing agent Also reductant, reducer, or electron donor. A chemical species that loses or donates one or more electrons to another species, called the oxidizing agent, in a redox reaction, thereby causing the reduction of the other species and in turn being itself oxidized. The reducing agent's oxidation state increases, while the oxidizing agent's decreases.
If the aqueous solution is saturated with a given salt solute, any additional such salt precipitates out of the solution. In the more general Brønsted–Lowry acid–base theory (1923), a base is a substance that can accept hydrogen cations (H+)—otherwise known as protons. This does include aqueous hydroxides since OH− does react with H+ to form water, so that Arrhenius bases are a subset of Brønsted bases. However, there are also other Brønsted bases which accept protons, such as aqueous solutions of ammonia (NH3) or its organic derivatives (amines). These bases do not contain a hydroxide ion but nevertheless react with water, resulting in an increase in the concentration of hydroxide ion. Also, some non-aqueous solvents contain Brønsted bases which react with solvated protons. For example, in liquid ammonia, NH2− is the basic ion species which accepts protons from NH4+, the acidic species in this solvent. G. N. Lewis realized that water, ammonia, and other bases can form a bond with a proton due to the unshared pair of electrons that the bases possess. In the Lewis theory, a base is an electron pair donor which can share a pair of electrons with an electron acceptor which is described as a Lewis acid. The Lewis theory is more general than the Brønsted model because the Lewis acid is not necessarily a proton, but can be another molecule (or ion) with a vacant low-lying orbital which can accept a pair of electrons. One notable example is boron trifluoride (BF3). Some other definitions of both bases and acids have been proposed in the past, but are not commonly used today.
Sources: en.wikipedia.org
Preanalytical factors such as sample type, time to processing, and stabilization method can change GSH and GSSG amounts. Analytical method and calibration also contribute to variation. Comparing absolute values across studies requires caution.
These assays typically measure total glutathione after oxidizing or reducing steps convert GSSG to GSH. A colorimetric or fluorometric signal is proportional to the recycling reaction. They generally do not report GSH and GSSG separately unless additional steps are used.
Solutions are often prepared fresh and kept cold, with protection from light and oxygen exposure. Chelating agents may reduce metal-catalyzed oxidation. Storage recommendations vary by buffer, pH, and concentration, so protocol-specific guidance should be followed.
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.