If you have been reading about LC-MS/MS and want a single page that covers the useful parts, this is it: definitions, context, how it is studied, and the questions that come up repeatedly.
Last reviewed on 2025-10-12. Where a claim depends on a specific study, the study is described rather than over-claimed.
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.
Quality control for glutathione measurements includes calibration with authenticated standards, internal standards where available, blank correction, and spike recovery checks. Because glutathione can form during sample processing or degrade before analysis, pre-analytical handling is a major source of variability. Interlaboratory comparisons often show differences in reported values due to method-specific calibration and detection principles. Interpretive thresholds are context-dependent, and no single reference range applies across all tissues or matrices. Researchers generally report both reduced and oxidized forms, along with the method and sample handling details.
Quantification of glutathione in biological or food samples commonly uses liquid chromatography coupled to ultraviolet, fluorescence, electrochemical, or mass spectrometric detection. Because the thiol group oxidizes readily, samples are often acidified or derivatized immediately after collection to stabilize reduced glutathione. Enzymatic recycling assays and colorimetric kits offer higher throughput but generally lower specificity than chromatographic methods. Mass spectrometry can distinguish glutathione from related thiols and allow simultaneous measurement of oxidized forms. Reported concentrations depend strongly on sample type, extraction procedure, and analytical platform.
Glutathione reference materials are sensitive to oxygen, light, and elevated temperature. Solid material is typically stored desiccated at -20 °C or below, while solutions require tighter control because thiol oxidation proceeds faster in liquid form. Aqueous solutions are often prepared fresh, kept cold, and protected from air; some protocols add acid or chelating agents to slow metal-catalyzed oxidation. Repeated freeze-thaw cycles can accelerate degradation and should be avoided. Stability data vary by matrix, so laboratories usually verify performance with their own storage conditions.
| Property | Value | Notes |
|---|---|---|
| Chemical formula | C10H17N3O6S | Reduced form (GSH) |
| Molar mass | 307.32 g/mol | For GSH; GSSG is 612.63 g/mol |
| Appearance | White crystalline powder | Usually lyophilized |
| Solubility in water | Freely soluble (≥100 mg/mL) | pH dependent |
| Typical storage | -20 °C, desiccated | Protect from light and oxygen |
Storage conditions strongly influence glutathione stability. The solid reduced form is commonly kept desiccated at or below minus twenty degrees Celsius, protected from light and moisture. Aqueous solutions are less stable because the thiol group reacts with dissolved oxygen, and oxidation accelerates at neutral or alkaline pH. Acidic solutions and oxygen-free handling can slow degradation, but repeated freeze-thaw cycles should be avoided. Researchers often verify concentration before use, because apparent losses can arise from oxidation or water uptake.
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.
Quality control for glutathione materials checks identity, assay, purity, water content, and disulfide content. Commercial products vary from research-grade powder to dietary supplements, and labels may not distinguish reduced from oxidized forms. In the United States, oral glutathione is commonly sold as a dietary supplement rather than an approved drug, while injectable forms fall under different rules and may require a prescription. Regulatory status differs by country. Analytical certificates, when available, help verify what a material contains, but independent testing remains important for interpretation.
Laboratory measurement of glutathione typically starts with rapid acid extraction to prevent oxidation and enzymatic degradation. Common methods include enzymatic recycling assays, high-performance liquid chromatography, and liquid chromatography coupled with mass spectrometry. The recycling assay uses glutathione reductase and a thiol-reactive colorimetric or fluorescent reagent, measuring total glutathione after converting disulfide forms. Chromatographic methods can separate reduced and oxidized forms, which helps when the redox ratio is the target. Choice of method affects sensitivity, specificity, and the amount of sample needed.
Samples for glutathione analysis require careful handling because the compound oxidizes readily and can be consumed by enzymes after collection. Blood is often treated with acid or thiol-blocking agents soon after draw, and plasma should be separated quickly from red blood cells. Tissues are usually snap-frozen or extracted immediately. Aqueous solutions of glutathione are less stable than dry powder and degrade faster at neutral or alkaline pH, in light, or with dissolved oxygen. Repeated freeze-thaw cycles also reduce reliability.
Storage recommendations for glutathione reagents usually specify a cool, dry, dark environment because the thiol oxidizes in air and light. Solid material is often kept desiccated at low temperature, while solutions are prepared fresh or stored frozen in aliquots. Repeated freeze-thaw cycles can accelerate degradation, and metal ions can catalyze oxidation. Quality control may include purity assays, water content, and identity confirmation. Stability limits are method-specific, so a stated shelf life applies only to defined conditions and packaging.
Laboratory measurement of glutathione requires attention to oxidation before analysis. Blood, tissue, or cell samples can lose reduced glutathione as it converts to GSSG or forms mixed disulfides with proteins. Acid extraction, rapid freezing, and thiol-blocking reagents are common strategies to preserve the original distribution. Reported concentrations therefore depend on collection protocol, extraction method, and the time between sampling and analysis. Comparisons across studies are most reliable when these pre-analytical variables are described.
Common analytical approaches include enzymatic recycling assays, high-performance liquid chromatography, and mass spectrometry. The enzymatic recycling assay uses glutathione reductase and a colorimetric or fluorometric reagent to amplify signal, which gives good sensitivity for total glutathione. Chromatographic methods can separate GSH from GSSG and related thiols, while mass spectrometry offers structural confirmation and multiplexing. Each approach has different requirements for calibration, internal standards, and validation. No single method captures every form of glutathione in every matrix.
== Human health == In addition to its significance for the field of evolutionary biology, de novo gene birth has implications for human health. It has been speculated that novel genes, including de novo genes, may play an outsized role in species-specific traits; however, many species-specific genes lack functional annotation. Nevertheless, there is evidence to suggest that human-specific de novo genes are involved in diseases such as cancer. NYCM, a de novo gene unique to humans and chimpanzees, regulates the pathogenesis of neuroblastomas in mouse models, and the primate-specific PART1, an lncRNA gene, has been identified as both a tumor suppressor and an oncogene in different contexts. Several other human- or primate-specific de novo genes, including PBOV1, GR6, MYEOV, and ELFN1-AS1, are also linked to cancer. Some have even suggested considering tumor-specifically expressed, evolutionary novel genes as their own class of genetic elements, noting that many such genes are under positive selection and may be neofunctionalized in the context of tumors. The specific expression of many de novo genes in the human brain also raises the intriguing possibility that de novo genes influence human cognitive traits. One such example is FLJ33706, a de novo gene that was identified in GWAS and linkage analyses for nicotine addiction and shows elevated expression in the brains of Alzheimer's patients. Further research, however, showed that FLJ33706 and other de novo gene candidates expressed in the human brain are either not translated or are diverged duplicates.
=== 1989 local government reforms === For many decades until the local government reforms of 1989, a borough with more than 20,000 people could be proclaimed a city. The boundaries of councils tended to follow the edge of the built-up area, so little distinction was made between the urban area and the local government area. New Zealand's local government structural arrangements were significantly reformed by the Local Government Commission in 1989 when approximately 700 councils and special purpose bodies were amalgamated to create 87 new local authorities. Regional councils were reduced in number from 20 to 13, territorial authorities (city/district councils) from 200 to 75, and special purpose bodies from over 400 to 7. The new district and city councils were generally much larger and most covered substantial areas of both urban and rural land. Many places that once had a city council were now being administered by a district council. As a result, the term "city" began to take on two meanings. City also came to be used in a less formal sense to describe major urban areas independent of local body boundaries. This informal usage is jealously guarded. Gisborne, for example, adamantly described itself as the first city in the world to see the new millennium. Gisborne is administered by a district council, but its status as a city is not generally disputed. Under current law, an urban area has to be at least 50,000 residents before it can be officially proclaimed as a city.
=== Mid-infrared === With the advent of cheap microcomputers it became possible to have a computer dedicated to controlling the spectrometer, collecting the data, doing the Fourier transform and presenting the spectrum. This provided the impetus for the development of FTIR spectrometers for the rock-salt region. The problems of manufacturing ultra-high precision optical and mechanical components had to be solved. A wide range of instruments are now available commercially. Although instrument design has become more sophisticated, the basic principles remain the same. Nowadays, the moving mirror of the interferometer moves at a constant velocity, and sampling of the interferogram is triggered by finding zero-crossings in the fringes of a secondary interferometer lit by a helium–neon laser. In modern FTIR systems the constant mirror velocity is not strictly required, as long as the laser fringes and the original interferogram are recorded simultaneously with higher sampling rate and then re-interpolated on a constant grid, as pioneered by James W. Brault. This confers very high wavenumber accuracy on the resulting infrared spectrum and avoids wavenumber calibration errors.
Alanine (symbol Ala or A), or α-alanine, is an α-amino acid that is used in the biosynthesis of proteins. It contains an amine group and a carboxylic acid group, both attached to the central carbon atom which also carries a methyl group side chain. Consequently it is classified as a non-polar, aliphatic α-amino acid. Under biological conditions, alanine exists in its zwitterionic form with its amine group protonated (as −NH+3) and its carboxyl group deprotonated (as −CO−2). Alanine is encoded by all codons starting with GC (GCU, GCC, GCA, and GCG). The L-isomer of alanine (left-handed) is the one that is incorporated into proteins. L-alanine is second only to L-leucine in rate of occurrence, accounting for 7.8% of the primary structure in a sample of 1,150 proteins. The right-handed form, D-alanine, occurs in peptides in some bacterial cell walls (in peptidoglycan) and in some peptide antibiotics, and occurs in the tissues of many crustaceans and molluscs as an osmolyte. Alanine is not an essential amino acid in humans because it can be synthesized metabolically and does not need to be present in the diet. However hypoalaninemia (alanine deficiency) is possible under certain conditions such as ketotic hypoglycemia.
Technetium exits the generator in the form of the pertechnetate ion, TcO4−. The oxidation state of Tc in this compound is +7. This is directly suitable for medical applications only in bone scans (it is taken up by osteoblasts) and some thyroid scans (it is taken up in place of iodine by normal thyroid tissues). In other types of scans relying on 99mTc, a reducing agent is added to the pertechnetate solution to bring the oxidation state of the technecium down to +3 or +4. Secondly, a ligand is added to form a coordination complex. The ligand is chosen to have an affinity for the specific organ to be targeted. For example, the exametazime complex of Tc in oxidation state +3 is able to cross the blood–brain barrier and flow through the vessels in the brain for cerebral blood flow imaging. Other ligands include sestamibi for myocardial perfusion imaging and mercapto acetyl triglycine for MAG3 scan to measure renal function.
Sources: en.wikipedia.org
=== Later work === In 1965, Zuckerkandl moved back to France to direct in Montpellier, the "Centre de Recherche de Biochimie Macromoléculaire" of the Centre National de Recherche Scientifique. In 1971, he became the founding editor of the Journal of Molecular Evolution, and in the late 1970s became President of the Linus Pauling Institute (then in 1992 of its successor, the Institute of Molecular Medical Sciences). His recent work includes criticism of social constructionism and intelligent design.
== Side effects == The most common side effects include lymphadenopathy (swollen lymph nodes), itching, pain, oedema, and bleeding (for example in the form of bruises or ecchymoses). Allergic reactions are seen in less than 1% of patients. In Peyronie's disease, potential side effects include corporal rupture (penile fracture) or other serious penile injury.
=== Other devices === The Endocare PerCryo Percutaneous Cryoablation device utilizes argon as a coolant and can be used with four different single cryoprobe configurations with a diameter of either 1.7 mm (~16 gauge) or 2.4 mm (~13 gauge) in diameter . The Myoscience (acquired by Pacira in 2019) Iovera is a handheld device that uses nitrous oxide as a coolant and can be used with a three-probe configuration with a probe diameter of 0.4 mm (~27 gauge).
The monocled cobra (Naja kaouthia) is a medically important species as it is responsible for a considerable number of bites throughout its range. The major toxic components in the Monocled cobras venom are postsynaptic neurotoxins, which block the nerve transmission by binding specifically to the nicotinic acetylcholine receptor, leading to flaccid paralysis and even death by respiratory failure. The major α-neurotoxin in Naja kaouthia venom is a long neurotoxin, α-cobratoxin; the minor α-neurotoxin is different from cobrotoxin in one residue. The neurotoxins of this particular species are weak. The venom of this species also contains myotoxins and cardiotoxins. The median lethal dose (LD50) is 0.28–0.33 mg per gram of mouse body weight. In case of IV the LD50 is 0.373 mg/kg, and 0.225 mg/kg in case of IP. The average venom yield per bite is approximately 263 mg (dry weight). The monocled cobra causes the highest fatality due to snake venom poisoning in Thailand. Envenomation usually presents predominantly with extensive local necrosis and systemic manifestations to a lesser degree. Drowsiness, neurological and neuromuscular symptoms will usually manifest earliest; hypotension, flushing of the face, warm skin, and pain around bite site typically manifest within one to four hours following the bite; paralysis, ventilatory failure or death could ensue rapidly, possibly as early as 60 minutes in very severe cases of envenomation. However, the presence of fang marks does not always imply that envenomation actually occurred.
Probable UIP pattern: Predominantly subpleural and basal Often heterogenous distribution Reticular pattern with peripheral traction bronchiectasis or bronchiolectasis There may be mild ground-glass opacity Indeterminate for UIP: Predominantly subpleural and basal Subtle reticular pattern May have mild ground-glass opacity or distortion (“early UIP pattern”) Findings suggestive of another diagnosis, including: Other predominant distribution: Peribronchovascular Perilymphatic Upper or mid-lung Cysts Marked mosaic pattern Predominant ground-glass opacity Profuse lung micronodules Lung nodules, especially centrilobular Consolidation Pleural plaques (indicating asbestosis) Dilated esophagus (indicating connective tissue disease) Distal clavicular erosions (indicating rheumatoid arthritis) Extensive lymph node enlargement Pleural effusion Pleural thickening (indicating connective tissue disease/drugs)
Sources: en.wikipedia.org
The regeneration fibers must cross the injury site and regeneration through the proximal or retrograde area of degeneration may require several weeks. Then the neuritis tip progresses down the distal site, such as the wrist or hand. Proximal lesion may grow distally as fast as 2 to 3 mm per day and distal lesion as slowly as 1.5 mm per day. Regeneration occurs over weeks to years.
April 2022: The Central Licensing Authority, DCGI granted avipatdil manufacturing and marketing permission to Zuventus Healthcare Ltd under the brand name 'Oxyptadil', for treatment in patients with severe COVID-19 with ARDS.
In 1887 Johannes Wislicenus published a study of stereoisomerism in unsaturated compounds. Groth made a systematic classification of minerals based on their chemical composition and crystal structure and published his results in his 5-volume Chemische Kristallographie in 1906–1919, which contained crystalline morphology and physical property data on nearly 10,000 substances. In 1913 Walter Wahl summarised the known connections between chemical composition and crystalline form as isomorphism (Mitscherlich), morphotropism (Groth), and enantiomorphism (Pasteur and van 't Hoff). In his preface to Andreas Fock's An introduction to chemical crystallography Pope summarised the state of chemical crystallography in 1895 as follows:
=== 16 April === Ukraine and Russia conducted an Orthodox Easter prisoner swap. Some one hundred and thirty Ukrainian POWs were returned to Ukraine in exchange for an unknown number of Russian soldiers. Ukrainian officials said that the remains of some eighty-two deceased Ukrainian soldiers were retrieved from territory controlled by Russia. Chinese defense minister Li Shangfu met with Putin amid reports of Ukrainian forces finding an increasing number of Chinese components in Russian weapons, and leaked classified documents from the United States about China's alleged plans to covertly supply Russia with weapons.
Compared to laser phototherapy, Light Emitting Diode Therapy (LEDT) is recognized for its enhanced safety profile, exhibiting fewer short-term and long-term side effects. This distinction stems from LEDT's use of non-coherent light at lower intensities, which minimizes the risks of tissue damage and discomfort often associated with the high-intensity, coherent light of lasers. Still, there are some side effects that can be commonly seen after exposure to light, that vary on the therapy patients take, PBMT or PDT.
Sources: en.wikipedia.org
Glutathione is a tripeptide of three amino acids: glutamate, cysteine, and glycine. The cysteine residue provides the sulfhydryl group that gives the molecule its reducing properties.
GSH is the reduced form, which contains a free sulfhydryl group. GSSG is the oxidized form, formed when two GSH molecules join through a disulfide bond. The ratio of GSH to GSSG is often used to assess cellular redox status.
No, glutathione is synthesized endogenously in most cells. It is not classified as an essential nutrient because the body can produce it from amino acid precursors. Dietary sources exist, but they are not required to maintain life.
Acidification lowers pH and helps prevent oxidation of the thiol group during extraction and storage. It can also precipitate proteins and stabilize the reduced form before analysis.