glutathione comes up often in conversation and rarely with the context attached. Here we lay out the basics in order, then work through the practical considerations.
Last reviewed on 2025-08-21. Where a claim depends on a specific study, the study is described rather than over-claimed.
Measuring glutathione requires attention to oxidation during sample handling, because GSH in biological samples can convert to GSSG or form mixed disulfides with proteins after collection. Acidic extraction, rapid cooling, and chelating agents are commonly used to limit such changes. Analytical methods usually distinguish free reduced glutathione, total glutathione, and protein-bound forms. Because these forms have different stability and reactivity, reported values depend heavily on the preparation protocol. No single preparation is universally suitable for every biological matrix or analytical goal.
Several techniques are used for quantification. Enzymatic recycling assays rely on glutathione reductase and a colorimetric or fluorescent readout, offering sensitivity for total glutathione. High-performance liquid chromatography can separate GSH from GSSG and other thiols, often with UV, fluorescence, or electrochemical detection. Mass spectrometry provides structural confirmation and can quantify low-abundance species when paired with separation. Each approach has trade-offs in specificity, throughput, and equipment requirements, so method selection depends on the research question and available instrumentation.
Stability depends on pH, temperature, oxygen exposure, and trace metals. Aqueous solutions of reduced glutathione are susceptible to oxidation, especially when neutral or alkaline and exposed to air. Transition metal ions can catalyze thiol oxidation, so chelators and inert atmospheres are sometimes used in research settings. Standards are typically stored cold and desiccated, with limited freeze-thaw cycles. Questions remain about how closely in vitro stability data reflect the behavior of glutathione within intact cells and tissues.
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.
| Property | Value | Notes |
|---|---|---|
| Reduced form | GSH | Main intracellular thiol |
| Oxidized form | GSSG | Disulfide dimer of two GSH molecules |
| Common separation method | Reversed-phase HPLC | Often with ion-pairing or derivatization |
| Typical detection | Fluorescence or mass spectrometry | UV detection is also used in some assays |
| Storage of standards | -20 °C or below, desiccated | Limit freeze-thaw and moisture exposure |
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.
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.
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.
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.
Tempeh begins with whole soybeans, which are softened by soaking, dehulled, then partly cooked. Specialty tempeh may be made from other types of beans, wheat, or may include a mixture of beans and whole grains. Adding vinegar during soybeans soaking process had also been reported in tempeh industries and it had been found to influence the sensory nature of the final product. The principal step in making tempeh is the fermentation of soybeans which undergo inoculation with Rhizopus spp. molds, a type of filamentous fungus most widely used for the production of tempeh. A fermentation starter containing the spores of fungus Rhizopus oligosporus or Rhizopus oryzae is mixed in. The beans are spread into a thin layer and are allowed to ferment for 24 to 36 hours at a temperature around 30°C (86°F). The soybeans have to cool down to allow spore germination and abundant growth of mycelium. Later, the temperature of the beans will naturally rise and rapid mold growth happens for around 4 hours. As mold growth declines, the soybeans should be bound into a solid mass by the mycelium. In good tempeh, the beans are knitted together by a mat of white mycelium. Typically, tempeh is harvested after 48 hours of fermentation with its distinguishable whitish color, firm texture, and nutty flavor. Extended fermentation time results in an increase in pH and undesirable color darkening in the tempeh.
=== Custom Tags === ColdFusion provides several ways to implement custom markup language tags, i.e. those not included in the core ColdFusion language. These are especially useful for providing a familiar interface for web designers and content authors familiar with HTML but not imperative programming. The traditional and most common way is using CFML. A standard CFML page can be interpreted as a tag, with the tag name corresponding to the file name prefixed with "cf_". For example, the file IMAP.cfm can be used as the tag "cf_imap". Attributes used within the tag are available in the ATTRIBUTES scope of the tag implementation page. CFML pages are accessible in the same directory as the calling page, via a special directory in the ColdFusion web application, or via a CFIMPORT tag in the calling page. The latter method does not necessarily require the "cf_" prefix for the tag name. A second way is the developments of CFX tags using Java or C++. CFX tags are prefixed with "cfx_", for example "cfx_imap". Tags are added to the ColdFusion runtime environment using the ColdFusion administrator, where JAR or DLL files are registered as custom tags. Finally, ColdFusion supports JSP tag libraries from the JSP 2.0 language specification. JSP tags are included in CFML pages using the CFIMPORT tag.
It has been proposed that ubiquitin is the slowest-evolving protein identified to date. Ubiquitin contains seven lysine residues to which another ubiquitin can be ligated, resulting in different types of polyubiquitin chains. Chains in which each additional ubiquitin is linked to lysine 48 of the previous ubiquitin have a role in proteasome targeting, while other types of chains may be involved in other processes.
Sources: en.wikipedia.org
== Committees == CLSI documents are developed by committees consisting of experts in medical testing or related aspects. Each CLSI committee produces consensus documents related to a specific discipline.
== Prizes and awards == 2023: VinFuture, Innovators with Outstanding Achievements in Emerging Fields – Jens Juul Holst, Joel Francis Habener, Daniel Joshua Drucker and Svetlana Mojsov 2023: Nature 10 most influential people who shaped science 2024: Pearl Meister Greengard Prize by the Rockefeller University 2024: Time 100 Most Influential People, Pioneers section 2024: Princess of Asturias Awards, Technical and Scientific Research – Daniel J. Drucker, Jeffrey M. Friedman, Joel F. Habener, Jens Juul Holst and Svetlana Mojsov 2024: Tang Prize, Biopharmaceutical Science – Joel F. Habener, Svetlana Mojsov and Jens Juul Holst 2024: Lasker-DeBakey Clinical Medical Research Award – Joel Habener, Svetlana Mojsov and Lotte Bjerre Knudsen 2024: BBVA Foundation Frontiers of Knowledge Awards - Biology and Biomedicine - Daniel Joshua Drucker, Joel Habener, Jens Juul Holst and Svetlana Mojsov 2025: Breakthrough Prize in Life Sciences - Daniel J. Drucker, Joel Habener, Jens Juul Holst, Lotte Bjerre Knudsen and Svetlana Mojsov; Alberto Ascherio and Stephen L. Hauser; and David R. Liu 2025: Warren Triennial Prize – Joel Habener, Daniel J.
=== Menopausal hormone therapy === CPA is used at low doses in menopausal hormone therapy in combination with an estrogen to provide endometrial protection and treat menopausal symptoms. It is used in menopausal hormone therapy under the brand name Climen, which is a sequential preparation that contains 2 mg estradiol valerate and 1 mg CPA. Climen was the first product for use in menopausal hormone therapy containing CPA to be marketed. It is available in more than 40 countries.
=== Biosynthesis === The biosynthesis of the rapamycin core is accomplished by a type I polyketide synthase (PKS) in conjunction with a nonribosomal peptide synthetase (NRPS). The domains responsible for the biosynthesis of the linear polyketide of rapamycin are organized into three multienzymes, RapA, RapB, and RapC, which contain a total of 14 modules (figure 1). The three multienzymes are organized such that the first four modules of polyketide chain elongation are in RapA, the following six modules for continued elongation are in RapB, and the final four modules to complete the biosynthesis of the linear polyketide are in RapC. Then, the linear polyketide is modified by the NRPS, RapP, which attaches L-pipecolate to the terminal end of the polyketide, and then cyclizes the molecule, yielding the unbound product, prerapamycin.
Sources: en.wikipedia.org
Common methods include enzymatic recycling assays, liquid chromatography, and mass spectrometry. Many protocols separate reduced glutathione from its oxidized disulfide form before detection.
The ratio compares reduced glutathione with its oxidized dimer. It is used as an indicator of redox status, although the value depends strongly on sample handling and analytical method.
Glutathione can oxidize quickly after a sample is collected. Acidification, cooling, and chelators are often used to reduce artifactual changes before analysis.
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.