Glutathione (GSH) is an antioxidant present in almost every cell in the body. It is a tri-peptide made up of the amino acids glycine, glutamic acid and cysteine in two consecutive reaction steps. Because it can be formed from these amino acids, glutathione is not considered an essential nutrient in the diet. Instead, glutathione production occurs within the cell, making it a key antioxidant for cellular metabolism, energy production. Glutathione is also a major cellular thiol participating in cellular redox reactions and thioether formation. It plays a role in the detoxification of drugs and xenobiotics, maintains and protects mitochondria for energy production in cells. GSH functions in Phase II of detoxication, leading to sequential modification, biliary excretion, and interorgan transport for final renal excretion, i.e., the mercapturate pathway which leads to liver detoxification. GSH has a role in signal transduction, in gene expression, and in apoptosis which will ultimately help in preventing carcinogenesis. Furthermore, reduced glutathione (GSH) acts as a hydrogen donor in the detoxification of hydrogen peroxide. In the human body, glutathione exists in two forms, 1. reduced and 2. oxidized (GSSG), which can be readily converted to each other. As a dietary supplement, GSH possesses various systemic effects such as improvement of liver abnormalities, improvement of diabetic complication,protection from viral infection, and antitumor activity. It is even used to treat autism.
Glutathione, is a thiol compound and its one of the regulators of melanogenic pathway in the human system due to which it has skin-lightening and anti-aging properties on skin. Also Glutathione increase the antioxidant capacity of cells, giving them a defence against free radical damage produced or generated due to internal and external factors.
Glutathione was discovered by J. de Rey-Paihade in 1888 from extracts of yeast and many animal tissues (beef skeletal muscle and liver, fish skeletal muscle, lamb small intestine, and sheep brain) and in fresh egg white. de Rey-Paihade named this substance philothion meaning love and sulfur in Greek. In 1921, Hopkins suggested that the philothion isolated from liver, skeletal muscle, and yeast is a dipeptide consisting of cysteine and glutamate but these authors overlooked the presence of glycine in philothion possibly due to misinterpretation of the Van Slyke amino N data. Honoring the history of the discovery of philothion, Hopkins named the substance “glutathione.” Based on the content of nitrogen and sulfur in Glutathione isolated from yeast, blood, and liver, Hunter and Eagles indicated in 1927 that Glutathione is not a dipeptide containing Glutamate–Cysteine but is a tripeptide consisting of Glutamate–Cysteine and an additional lowmolecular-weight amino acid (possibly serine). Using an acid hydrolysate of Glutathione, Hopkins proposed in 1929 that Glutathione is a tripeptide formed from cysteine, glutamate, and glycine. This proposal was supported by the independent work of Kendall and coworkers in 1929 and 1930.
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1. Guoyao Wu, Yun-Zhong Fang, Sheng Yang, Joanne R. Lupton and Nancy D. Turner. (2004) Glutathione Metabolism and Its Implications for Health. The Journal of Nutrition, 134(3) 489–492.
2. Kidd.P. (1997) Glutathione: Systemic Protectant Against Oxidative and Free Radical Damage. Alternative Medicine Review, Vol 2(3).
3. Arjinpathana N, Asawanonda P (2012) Glutathione as an oral whitening agent: a randomized, double-blind, placebo-controlled study. J Dermatolog Treat, 23(2):97-102.
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