Description
Glutathione reductase (GR) is a crucial flavoenzyme in the antioxidant defense system. Reduced glutathione (GSH) is used by glutathione peroxidase to detoxify hydrogen peroxide and in the precess 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, lipecalins, and α/β hydrolases. GR is stimulated by melatonin and is reportedly irreversibly inhibited by a number of oxygen radical generating systems.
Abbr
GR, Recombinant (E. coli)
Form
3.2 M ammonium sulphate
Enzyme Commission Number
EC 1.8.1.7
Activity
35 U/mg protein, 98 U/ml.
Molecular Weight
49.5 kDa
Purity
>95% as judged by SDS-PAGE
Unit Definition
One Unit of glutathione reductase was defined as the amount of enzyme responsible for the oxidation of 1 µmole of NADPH at 25 °C and pH 7.5.
Optimum temperature
25 °C
Storage
Glutathione reductase should be stored at 4 °C or and will remain stable up to 3 years if stored as specified.
Synonyms
GR; glutathione reductase; glutathione reductase (NADPH); NADPH-glutathione reductase; GSH reductase; GSSG reductase; NADPH-GSSG reductase; glutathione S-reductase; NADPH:oxidized-glutathione oxidoreductase
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