Other name: Glutathione(Oxidized Form), free acid; Oxidized glutathione；Oxiglutatione；Glutathione disulfide；N-(N-g-Glutamyl-cysteinyl)glycine-(2,2)-disulfide；Oxidized L-glutathione
N,N'-(Dithiobis(1-((carboxymethyl)carbamoyl)ethylene))di-L-glutamine；L-Oxidized glutathione；Glutathiol；glutathiondisulphide；Bis(γ-glutamyl-L-cysteinylglycine) disulfide
MP: 178 °C (dec.)(lit.)
Appearance: white powder
Solubility: soluble in water
Package: 100g, 1Kg, 25Kg
Applications: raw material for pharmaceuticals, feed and food
Glutathione is not an essential nutrient for humans, since it can be synthesized in the body from the amino acids L-cysteine, L-glutamic acid, and glycine; it does not have to be present as a supplement in the diet. The sulfhydryl group (SH) of cysteine serves as a proton donor and is responsible for its biological activity. Cysteine is the rate-limiting factor in cellular glutathione biosynthesis, since this amino acid is relatively rare in foods.
Glutathione exists in both reduced (GSH) and oxidized (GSSG) states. In the reduced state, the thiol group of cysteine is able to donate a reducing equivalent (H++ e−) to other molecules, such as reactive oxygen species to neutralize them, or to protein cysteines to maintain their reduced forms. With donating an electron, glutathione itself becomes reactive and readily reacts with another reactive glutathione to form glutathione disulfide (GSSG). Such a reaction is probable due to the relatively high concentration of glutathione in cells (up to 7 mM in the liver).
Both oxidized glutathione and reduced glutathione are available from UCEHM.