A practical reference on redox: what it is, how it behaves, what the literature reports, and where the honest uncertainties sit.
This page was last updated on 2026-03-27 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.
Accurate measurement of glutathione begins with careful sample handling. Because GSH oxidizes rapidly to GSSG, samples must be processed quickly or frozen immediately. Acid precipitation with metaphosphoric acid or perchloric acid is common; it lowers pH, precipitates proteins, and helps preserve the reduced form. Chelating agents such as EDTA can limit metal-catalyzed oxidation. For whole blood, hemolysis releases glutathione from erythrocytes, so plasma and serum values differ substantially from whole blood values.
Several analytical methods can quantify glutathione, including high-performance liquid chromatography (HPLC) with UV or fluorescence detection for separating GSH and GSSG. Liquid chromatography-tandem mass spectrometry (LC-MS/MS) offers higher specificity and sensitivity, often detecting nanomolar concentrations. The enzymatic recycling assay, often called the Tietze method, measures total glutathione by coupling reduction of GSSG to a colorimetric or fluorometric readout. Capillary electrophoresis and electrochemical detection are also used in specialized laboratories. Each method has distinct advantages and limitations regarding throughput, cost, and susceptibility to interference.
| 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 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.
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.
Working at the Royal Society in the 1660s, the physician Richard Lower began examining the effects of changes in blood volume on circulatory function and developed methods for cross-circulatory study in animals, obviating clotting by closed arteriovenous connections. The new instruments he was able to devise enabled him to perform the first reliably documented successful transfusion of blood in front of his distinguished colleagues from the Royal Society. According to Lower's account, "...towards the end of February 1665 [I] selected one dog of medium size, opened its jugular vein, and drew off blood, until its strength was nearly gone. Then, to make up for the great loss of this dog by the blood of a second, I introduced blood from the cervical artery of a fairly large mastiff, which had been fastened alongside the first, until this latter animal showed ... it was overfilled ... by the inflowing blood." After he "sewed up the jugular veins", the animal recovered "with no sign of discomfort or of displeasure". Lower had performed the first blood transfusion between animals. He was then "requested by the Honorable [Robert] Boyle ... to acquaint the Royal Society with the procedure for the whole experiment", which he did in December 1665 in the Society's Philosophical Transactions. The first blood transfusion from animal to human was administered by Jean-Baptiste Denys, eminent physician to King Louis XIV of France, on June 15, 1667. He transfused the blood of a sheep into a 15-year-old boy, who survived the transfusion.
Murphey went into cardiac arrest at the imaging unit following administration of the medication, and was transferred to an intensive care unit. After Murphey was transferred, Vaught informed other staff that she had administered vecuronium and admitted to several errors (with her admissions detailed in a Tennessee Bureau of Investigation investigative report). Murphey was placed on life support which was withdrawn the next day as a result of permanent brain death. Vaught was fired from the hospital after an internal investigation in January 2018 and was arrested and charged in Murphey's death in 2019.
Patrice Motsepe, businessman Herman Mashaba, businessman, president of ActionSA Mogoeng Mogoeng, former chief justice of South Africa Mamokgethi Phakeng, former vice chancellor of the University of Cape Town Tshepo Motsepe, businesswoman and first lady of South Africa Baaitse Nkabinde, former judge at the South African high court Refiloe Phoolo, musician and businessman Thato Sikwane, disk jockey and music producer Connie Ferguson, actress, film producer and businesswoman Motsi Mabuse, dancer and judge on Strictly Come Dancing
Sources: en.wikipedia.org
In the nineteenth century numerous authors described both cretinism and myxedema, and their relationship to the thyroid. Charles Mayo coined the term hyperthyroidism in 1910. Hakaru Hashimoto documented a case of Hashimoto's thyroiditis in 1912, antibodies in this disease were demonstrated in 1956. Knowledge of the thyroid and its conditions developed throughout the late nineteenth and twentieth centuries, with many modern treatments and investigative modalities evolving throughout the mid twentieth century, including the use of radioactive iodine, thiouracil and fine needle aspiration.
Meinhard I 1253–1258, also Count of Gorizia since 1231 Meinhard II 1258–1295, also Count of Gorizia until 1271, Duke of Carinthia and Margrave of Carniola from 1286, jointly with: Albert V 1258–1271, brother, also Count of Gorizia until 1304 Albert VI, son, until 1292 Henry II 1295–1335, son of Meinhard II, also Duke of Carinthia, King of Bohemia 1306 and 1307–1310, jointly with his brothers Louis, until 1305 Otto, until 1310 Male line extinct, Countess Margaret, daughter of Henry II, married to:
His position has mostly been met with negative comments across the media and sports press due to the NFL having as many as 4,500 former players reporting symptoms of CTE. More recently, he has been investigating the therapeutic effects of hyperbaric oxygen therapy (HBO) in various neurological conditions, including post-concussion syndrome, PTSD, traumatic brain injury, stroke, and spinal cord injury. Maroon was asked to testify to the New York City Council on a proposed rule on sideline medical coverage for organized youth football in the city. Together with Russell Blaylock, he developed an inflammation hypothesis for the biochemical mechanisms involved in the development of CTE following head trauma. In the 2015 movie Concussion, which "examines how American football players suffer from major head injuries and life-long debilitating problems as a result of repeated concussions, and efforts by the National Football League to deny it," Maroon was played by actor Arliss Howard. In the movie, Maroon is portrayed as an NFL-biased doctor who tries to deny any relationship between football concussions and the brain pathology that Dr. Bennet Omalu found and attributed to CTE. Since the release of the movie, several people have come forward in defense of Maroon, stating that his portrayal in the movie is sensationalized and incorrect.
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 oxidizes quickly when cells are disrupted or when samples sit at room temperature. Rapid processing or immediate freezing minimizes the conversion of GSH to GSSG. This step helps ensure that the measured ratio reflects the original biological state.