Description
Biochem/physiol Actions Glutathione reductase IGR） is a crucial flavoenzyme in the antioxidant defense system. Reduced glutathione （GSH） is used by glutathione peroxidase to detoxify hydrogen peroxide and in the process is converted to oxidized glutathione （GSSG）. The GSSG is then recycled back to GSH by glutathione reductase （GR） using NADPH that is then converted to NADP+. The regenerated GSH is then available to detoxify more hydrogen peroxide. The enzyme uses FAD as a cofactor. GR and glutathione peroxidase may inhibit lipid peroxidation by functioning as antioxidant enzymes in sperm. Glutathione reductase shares a structural motif with a number of other proteins including aspartyl proteases, citrate synthase, EF hands, hemoglobins, lipocalins, and α/β hydrolases. GR is stimulated by melatonin and is reportedly irreversibly inhibited by a number of oxygen radical generating systems.
Preparation Note Purified by affinity chromatography
Unit Definition One unit will reduce 1.0 μmole of oxidized glutathione per min at pH 7.6 at 25 °C.
Physical form Suspension in 3.6 M （NH4）2SO4, pH 7.0, containing 0.1 mM dithiothreitol
Properties
form ammonium sulfate suspension
mol wt mol wt 118 kDa
foreign activity G-6-PDH, 6-PGDH, and NADPH oxidase <0.01%
lipoamide dehydrogenase <0.1%
Gene Information bakers yeast ... GLR1（856014）
storage temp. 2-8°C
Safety
WGK Germany 2
References
reference Lenzi, A., et al., Glutathione treatment of dyspermia: effect on the lipoperoxidation process. Hum. Reprod. 9, 2044-2050, （1994）
Wan, W.Y., et al., A Natural Grouping of Motifs with an Aspartate or Asparagine Residue Forming Two Hydrogen Bonds to Residues Ahead in Sequence. J. Mol. Biol. 286, 1633-1649, （1999）
Reiter, R.J., et al., Reactive oxygen intermediates, molecular damage, and aging. Relation to melatonin. Ann. N.Y. Acad. Sci. 854, 410-424, （1998）
Gutierrez-Correa, J., and Stoppani, A.O., Inactivation of yeast glutathione reductase by Fenton systems: effect of metal chelators, catecholamines and thiol compounds. Free Radic. Res. 27, 543-555, （1997）
Printable Reviews
Product ReviewsReview This Product
