Glutathion
Glutathion Uses, Dosage, Side Effects, Food Interaction and all others data.
A tripeptide with many roles in cells. It conjugates to drugs to make them more soluble for excretion, is a cofactor for some enzymes, is involved in protein disulfide bond rearrangement and reduces peroxides.
| Trade Name | Glutathion |
| Generic | Glutathione |
| Glutathione Other Names | Glutathion, Glutathione, Glutathione-SH, Reduced glutathione |
| Type | |
| Formula | C10H17N3O6S |
| Weight | Average: 307.323 Monoisotopic: 307.083805981 |
| Groups | Approved, Investigational, Nutraceutical |
| Therapeutic Class | |
| Manufacturer | |
| Available Country | |
| Last Updated: | September 19, 2023 at 7:00 am |
Uses
For nutritional supplementation, also for treating dietary shortage or imbalance
Glutathion is also used to associated treatment for these conditions: Hangover, Nerve Disorders, Neuropathies
How Glutathion works
Glutathion (GSH) participates in leukotriene synthesis and is a cofactor for the enzyme glutathione peroxidase. It also plays a role in the hepatic biotransformation and detoxification process; it acts as a hydrophilic molecule that is added to other lipophilic toxins or wastes prior to entering biliary excretion. It participates in the detoxification of methylglyoxal, a toxic by-product of metabolism, mediated by glyoxalase enzymes. Glyoxalase I catalyzes the conversion of methylglyoxal and reduced glutathione to S-D-Lactoyl-glutathione. Glyoxalase II catalyzes the conversion of S-D-Lactoyl Glutathion to Reduced Glutathion and D-lactate. Glyoxalase I catalyzes the conversion of methylglyoxal and reduced glutathione to S-D-Lactoyl-glutathione. Glyoxalase II catalyzes the conversion of S-D-Lactoyl Glutathion to Reduced Glutathion and D-lactate. GSH is a cofactor of conjugation and reduction reactions that are catalyzed by glutathione S-transferase enzymes expressed in the cytosol, microsomes, and mitochondria. However, it is capable of participating in non-enzymatic conjugation with some chemicals, as it is hypothesized to do to a significant extent with n-acetyl-p-benzoquinone imine (NAPQI), the reactive cytochrome P450 reactive metabolite formed by toxic overdose of acetaminophen. Glutathion in this capacity binds to NAPQI as a suicide substrate and in the process detoxifies it, taking the place of cellular protein sulfhydryl groups which would otherwise be toxically adducted. The preferred medical treatment to an overdose of this nature, whose efficacy has been consistently supported in literature, is the administration (usually in atomized form) of N-acetylcysteine, which is used by cells to replace spent GSSG and allow a usable GSH pool.
Toxicity
ORL-MUS LD50 5000 mg/kg, IPR-MUS LD50 4020 mg/kg, SCU-MUS LD50 5000 mg/kg, IVN-RBT LD50 > 2000 mg/kg, IMS-MUS LD50 4000 mg/kg
Food Interaction
No interactions found.Elimination Route
Research suggests that glutathione is not orally bioactive, and that very little of oral glutathione tablets or capsules is actually absorbed by the body.
Innovators Monograph
You find simplified version here Glutathion
