Glutathione reduced

Glutathione is a tripeptide made up of the amino acids glutamic acid, cysteine, and glycine. The primary biological function of glutathione is to act as a non-enzymatic reducing agent to help keep cysteine thiol side chains in a reduced state on the surface of proteins. Glutathione is also used to prevent oxidative stress in most cells and helps to trap free radicals that can damage DNA and RNA. Affinity chromatography using glutathione-agarose permits rapid, mild, non-denaturing and highly selective purification of proteins containing glutathione binding sequences, such as glutathione S-transferase (GST), glutathione peroxidase and glyoxalase I. 1. Simons P.C., Vander Jagt D.L., Purification of glutathione S-transferases from human liver by glutathione-affinity chromatography. Anal. Biochem. 1977, 82, 334. 2. Simons P.C., Vander Jagt D.L., Purification of glutathione S-transferases by glutathione-affinity chromatography. Methods Enzymol. 1981, 77, 235. 3. Toribio F., Methods for purification of glutathione peroxidase and related enzymes. J. Chromatogr. 1996, 684, 77. 4. Wu G., Fang Y.Z., Yang S., Lupton J.R., Turner N.D., Glutathione metabolism and its implications for health. J. Nutr. 2004, 134, 489-92.