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Total products in Glutathione: 3 | Page 1 of 1 |
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While all cells in the human body are capable of synthesizing glutathione, liver glutathione synthesis has been shown to be essential. Following birth, mice with genetically-induced loss of GCLC (i.e., GSH synthesis) only in the liver die within 1 month of birth. The biosynthesis pathway for glutathione is found in some bacteria, like cyanobacteria and proteobacteria, but is missing in many other bacteria. Most eukaryotes synthesize glutathione, including humans, but some do not, such as Leguminosae, Entamoeba, and Giardia. The only archaea that make glutathione are halobacteria.
Glutathione maintains proper oxidation-reduction (redox) potential inside cells. Redox affects the oxidation state of sulfur in enzymes, and thus affects the rates of biochemical reactions in cells. It also scavenges peroxides and oxidizing free radicals directly and also serves as the basis for the antioxidant network. Glutathione stores and transports cysteine throughout the body.
Glutathione exists in reduced and oxidized states. In the reduced state, the thiol group of cysteine is able to donate a reducing equivalent to other unstable molecules, such as reactive oxygen species. In donating an electron, glutathione itself becomes reactive, but readily reacts with another reactive glutathione to form glutathione disulfide. Such a reaction is possible due to the relatively high concentration of glutathione in cells. GSH can be regenerated from GSSG by the enzyme glutathione reductase.
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