Introduction
Glutathione (GSH) refers to a tripeptide that constitutes an odd peptide that links the carboxyl group of the glutamate side-chain and the amine group of cysteine (Sakamoto et al, 1983). GSH is an antioxidant, therefore it shields important cellular components from damage brought about by reactive oxygen species like peroxides or free radicals. Thiol groups which are found existing at a concentration of around 5 mM in animal cells are typically reducing agents. By functioning as an electron donor glutathione reduces inside cytoplasmic proteins to cysteines. As a result of the process, glutathione disulfide (GSSG) (oxidized form of glutathione) is formed from the conversion of glutathione.the following explores the importance of GSH to the body and how its levels can be boosted within the body (Sakamoto et al, 1983).
Glutathione exists solely in its reduced form, this is because glutathione reductase an enzyme that is responsible for reverting it from its oxidized form, upon oxidative stress is constitutively inducible and active. Cellular toxicity is commonly measured by the ratio of reduced glutathione to that of oxidized glutathione inside animal cells.Glutathione can be synthesized inside the body from l-glutamic acid, glycine and L-cysteine (amino acids) hence GSH is not an essential nutrient because it does not have to be extracted from food. Not only does the sulfhydryl (thiol) group (SH) of cysteine serve the purpose of donating protons but they are also behind the biological activity of glutathione. The rate of glutathione synthesis in the cells is depended on the provision of this amino acid, given that cysteine is rather rare in food. Moreover, if cysteine is released as the free amino acid, it is toxic and it’s impulsively catabolized in the intestines and blood plasma(Arias & Jakoby, 1976).
Structure of glutathione
-The melting point of GSH is 195 degrees celcius
-Molar mass: 307.3235 g/mol
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