This is a working overview of derivatization, written for readers who want more than a one-paragraph summary but less than a textbook.
This page was last updated on 2025-09-28 and is reviewed periodically as new material appears.
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 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.
Commercial glutathione is produced by microbial fermentation or chemical synthesis, then purified. Reduced and oxidized grades are offered separately, with purity specifications often exceeding 98 percent. The compound appears in foods such as fresh fruits, vegetables, and meats, although cooking and processing can lower amounts. Oral, topical, and inhaled forms are discussed in research and consumer contexts, but absorption and tissue delivery remain active areas of study. Regulatory status varies by country and intended use.
Glutathione is a small sulfur-containing peptide built from glutamic acid, cysteine, and glycine. Its distinctive feature is a gamma-glutamyl bond between glutamate's side-chain carboxyl group and cysteine's amino group. This linkage resists ordinary peptidases and helps the molecule remain stable inside cells. The reduced thiol form, often abbreviated GSH, is the dominant intracellular species. The oxidized disulfide dimer, GSSG, forms when two reduced molecules link through their cysteine sulfur atoms. The balance between these forms is a common redox indicator.
In living systems, glutathione occurs in millimolar concentrations in many cell types, while extracellular levels are generally much lower. The liver holds a substantial share of the body's total pool, and the molecule participates in reduction, detoxification, and amino acid transport. It also serves as a cofactor for enzymes such as glutathione peroxidase and glutathione S-transferase. Because the cysteine residue supplies a reactive thiol, glutathione can donate electrons and become oxidized. Cells regenerate reduced glutathione through glutathione reductase using NADPH.
| 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 |
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.
Measuring glutathione in biological samples requires attention to oxidation and matrix effects. High-performance liquid chromatography with ultraviolet or fluorescence detection can separate reduced and oxidized forms after derivatization. Liquid chromatography with tandem mass spectrometry offers higher specificity and can quantify glutathione alongside related thiols. Because glutathione can oxidize during sample handling, many protocols use rapid acidification with metaphosphoric acid or sulfosalicylic acid. Internal standards help correct for losses during extraction and analysis.
Enzymatic recycling assays provide a complementary approach for total glutathione. In these methods, glutathione reductase reduces oxidized glutathione while a thiol-reactive reagent, such as 5,5'-dithiobis(2-nitrobenzoic acid), produces a colored product. The reaction cycles between reduced and oxidized forms, amplifying the signal. Spectrophotometric or fluorometric detection can then estimate concentration. Distinguishing reduced glutathione from glutathione disulfide often requires separate aliquots, masking agents, or chromatographic separation, and the choice affects reported values.
=== Norbornene cycloaddition === 1,3 dipolar cycloadditions have been developed as a bioorthogonal reaction using a nitrile oxide as a 1,3-dipole and a norbornene as a dipolarophile. Its primary use has been in labeling DNA and RNA in automated oligonucleotide synthesizers, and polymer crosslinking in the presence of living cells.
== 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.
== Function == The major role of IGF-2 is as a growth promoting hormone during gestation. IGF-2 exerts its effects by binding to the IGF-1 receptor and to the short isoform of the insulin receptor (IR-A or exon 11-). IGF-2 may also bind to the IGF-2 receptor (also called the cation-independent mannose 6-phosphate receptor), which acts as a signalling antagonist; that is, to prevent IGF-2 responses. In the process of folliculogenesis, IGF-2 is created by thecal cells to act in an autocrine manner on the theca cells themselves, and in a paracrine manner on granulosa cells in the ovary. IGF-2 promotes granulosa cell proliferation during the follicular phase of the menstrual cycle, acting alongside follicle stimulating hormone (FSH). After ovulation has occurred, IGF-2 promotes progesterone secretion during the luteal phase of the menstrual cycle, together with luteinizing hormone (LH). Thus, IGF-2 acts as a co-hormone together with both FSH and LH. A study at the Mount Sinai School of Medicine found that IGF-2 may be linked to memory and reproduction. A study at the European Neuroscience Institute-Goettingen (Germany) found that fear extinction-induced IGF-2/IGFBP7 signalling promotes the survival of 17- to 19-day-old newborn hippocampal neurons. This suggests that therapeutic strategies that enhance IGF-2 signalling and adult neurogenesis might be suitable to treat diseases linked to excessive fear memory such as PTSD.
=== Rotigotine === Rotigotine (sold under the brand name Neupro, among others) is a dopamine agonist indicated for the treatment of Parkinson's disease (PD) and restless legs syndrome (RLS). In 2007, the Neupro patch was approved by the Food and Drug Administration (FDA) as the first transdermal patch treatment of Parkinson's disease in the United States. The drug had been established in 1980, and no prior polymorphism had been observed. In 2008, a more stable polymorph unexpectedly emerged, which was described as resembling "snow-like crystals". The new polymorph did not display any observable reduction in efficacy, but nonetheless, Schwarz Pharma recalled all Neupro patches in the United States and some in Europe. Those with remaining patches in Europe were told to refrigerate their stock, since refrigeration seemed to reduce crystallization rates. The patch was reformulated in 2012, as per FDA recommendations, and was reintroduced in the United States without requiring refrigeration.
The precise reason why there are only four nucleotides is debated, but there are several unused possibilities. Furthermore, adenine is not the most stable choice for base pairing: in Cyanophage S-2L, diaminopurine (DAP) is used instead of adenine. Diaminopurine basepairs perfectly with thymine as it is identical to adenine but has an amine group at position 2 forming 3 intramolecular hydrogen bonds, eliminating the major difference between the two types of basepairs (weak A-T vs strong C-G). This improved stability affects protein-binding interactions that rely on those differences. Other combination include:
Sources: en.wikipedia.org
Severe respiratory instability Acute psychiatric instability Uncontrolled suicide risk Diagnosed non-nicotine substance abuse QTc intervals longer than 500 milliseconds if prescribed methadone Acute diversion of controlled substances Intolerance from previous trial use with specific opioids Serious adverse effects or lack of efficacy
=== Mechanism of action === As an adenosine nucleoside triphosphate analog (GS-443902), the active metabolite of remdesivir interferes with the action of viral RNA-dependent RNA polymerase and evades proofreading by viral exoribonuclease (ExoN), causing a decrease in viral RNA production. In some viruses, such as the respiratory syncytial virus, it causes the RNA-dependent RNA polymerases to pause, but its predominant effect (as in Ebola) is to induce an irreversible chain termination. Unlike with many other chain terminators, this is not mediated by preventing addition of the immediately subsequent nucleotide, but is instead delayed, occurring after five additional bases have been added to the growing RNA chain. For the RNA-dependent RNA polymerases of MERS-CoV, SARS-CoV-1, and SARS-CoV-2, arrest of RNA synthesis occurs after incorporation of three additional nucleotides. Hence, remdesivir is classified as a direct-acting antiviral agent that works as a delayed chain terminator.
=== Safety controversies and fraud === FDA staffers publicly complained that safety problems and some data integrity issues were ignored prior to approval, and the House Committee on Energy and Commerce held hearings to examine these complaints. One doctor went to prison because she falsified data in her portion of the clinical trials (about 400 patients out of 24,000). Further, Ketek seemed to cause liver problems, including "liver failure", to a greater extent than would be expected of a common-use antibiotic. The House Committee on Energy and Commerce held hearings. Study 3014 was a key clinical trial of approximately 24,000 patients which Sanofi-Aventis submitted to the FDA to seek approval for Ketek. The doctor who treated the most patients in Study 3014 (about 400), Maria "Anne" Kirkman Campbell, served a 57-month sentence in federal prison after pleading guilty to mail fraud, by defrauding Aventis and others. The indictment states that Campbell fabricated data she sent to the company. Documents, including internal Sanofi-Aventis emails show that Aventis was worried about Campbell early in study 3014 but didn't tell the FDA until the agency's own inspectors discovered the problem independently. In January 2006, an article in the March issue of Annals of Internal Medicine was published, citing three recent drug-induced liver injury cases likely due to telithromycin, one resulting in a liver transplant and one in death.
=== US and Canada === In the US, about half of all clinical psychology graduate students are being trained in PhD programs—a model that emphasizes research—with the other half in PsyD programs, which has more focus on practice (similar to professional degrees for medicine and law). Both models are accredited by the American Psychological Association and many other English-speaking psychological societies. A smaller number of schools offer accredited programs in clinical psychology resulting in a master's degree, which usually takes two to three years post-Bachelors. Although each of the US states is somewhat different in terms of requirements and licenses, there are three common elements:
Sources: en.wikipedia.org
Proteins can be informally divided into three main classes, which correlate with typical tertiary structures: globular proteins, fibrous proteins, and membrane proteins. Almost all globular proteins are soluble and many are enzymes. Fibrous proteins are often structural, such as collagen, the major component of connective tissue, or keratin, the protein component of hair and nails. Membrane proteins often serve as receptors or provide channels for polar or charged molecules to pass through the cell membrane. A special case of intramolecular hydrogen bonds within proteins, poorly shielded from water attack and hence promoting their own dehydration, are called dehydrons.
The human population exploits a large number of other animal species for food, both of domesticated livestock species in animal husbandry and, mainly at sea, by hunting wild species. Marine fish of many species are caught commercially for food. A smaller number of species are farmed commercially. Humans and their livestock make up more than 90% of the biomass of all terrestrial vertebrates, and almost as much as all insects combined. Invertebrates including cephalopods, crustaceans, insects—principally bees and silkworms—and bivalve or gastropod molluscs are hunted or farmed for food, fibres. Chickens, cattle, sheep, pigs, and other animals are raised as livestock for meat across the world. Animal fibres such as wool and silk are used to make textiles, while animal sinews have been used as lashings and bindings, and leather is widely used to make shoes and other items. Animals have been hunted and farmed for their fur to make items such as coats and hats. Dyestuffs including carmine (cochineal), shellac, and kermes have been made from the bodies of insects. Working animals including cattle and horses have been used for work and transport from the first days of agriculture. Animals such as the fruit fly Drosophila melanogaster serve a major role in science as experimental models. Animals have been used to create vaccines since their discovery in the 18th century. Some medicines such as the cancer drug trabectedin are based on toxins or other molecules of animal origin.
=== X-ray spectrometer === The most practical application of 244Cm—though rather limited in total volume—is as an α-particle source in alpha particle X-ray spectrometers (APXS). These instruments were installed on the Sojourner, Mars, Mars 96, Mars Exploration Rovers and Philae comet lander, as well as the Mars Science Laboratory to analyze the composition and structure of the rocks on the surface of planet Mars. APXS was also used in the Surveyor 5–7 moon probes but with a 242Cm source. An elaborate APXS setup has a sensor head containing six curium sources with a total decay rate of several tens of millicuries (roughly one gigabecquerel). The sources are collimated on a sample, and the energy spectra of the alpha particles and protons scattered from the sample are analyzed (proton analysis is done only in some spectrometers). These spectra contain quantitative information on all major elements in the sample except for hydrogen, helium and lithium.
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.
It is a tripeptide rather than a full protein. Proteins generally contain many amino acids joined by alpha-peptide bonds, while glutathione has three residues and an unusual gamma-glutamyl linkage. That structure affects how enzymes recognize and break it down.