Glutathione is a kind of antioxidant which donates electron continuously to cell membranes and protect from free radical toxins. This action goes on at all levels and any depletion of Glutathione leads to cell degeneration.
Please read more here:http://www.thorne.com/altmedrev/fulltext…http://en.wikipedia.org/wiki/Glutathione
Glutathione (GSH), whose IUPAC name is 2-amino-5-{[2-[(carboxymethyl)amino]- 1-(mercaptomethyl)-2-oxoethyl]amino}-5-o… acid, is γ-glutamylcysteinylglycine, a tripeptide. It contains an unusual peptide linkage between the amine group of cysteine and the carboxyl group of the glutamate side chain. Glutathione, an antioxidant, protects cells from toxins such as free radicals.[1]
Thiol groups are kept in a reduced state within ~5 mM in animal cells. In effect, glutathione reduces any disulfide bonds formed within cytoplasmic proteins to cysteines by acting as an electron donor. Glutathione is found almost exclusively in its reduced form, since the enzyme which reverts it from its oxidized form (GSSG), glutathione reductase, is constitutively active and inducible upon oxidative stress. In fact, the ratio of reduced to oxidized glutathione within cells is often used scientifically as a measure of cellular toxicity.
Glutathione is a kind of antioxidant which donates electron continuously to cell membranes and protect from free radical toxins. This action goes on at all levels and any depletion of Glutathione leads to cell degeneration.
Please read more here:http://www.thorne.com/altmedrev/fulltext…http://en.wikipedia.org/wiki/Glutathione
the wikipedia defines Glutathione but I found know mention as
a whitener? http://www.pdrhealth.com/drug_info/nmdru…
Glutathione (GSH), whose IUPAC name is 2-amino-5-{[2-[(carboxymethyl)amino]- 1-(mercaptomethyl)-2-oxoethyl]amino}-5-o… acid, is γ-glutamylcysteinylglycine, a tripeptide. It contains an unusual peptide linkage between the amine group of cysteine and the carboxyl group of the glutamate side chain. Glutathione, an antioxidant, protects cells from toxins such as free radicals.[1]
Thiol groups are kept in a reduced state within ~5 mM in animal cells. In effect, glutathione reduces any disulfide bonds formed within cytoplasmic proteins to cysteines by acting as an electron donor. Glutathione is found almost exclusively in its reduced form, since the enzyme which reverts it from its oxidized form (GSSG), glutathione reductase, is constitutively active and inducible upon oxidative stress. In fact, the ratio of reduced to oxidized glutathione within cells is often used scientifically as a measure of cellular toxicity.