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G1786 Sigma

Glutathione Reductase from bovine intestinal mucosa

lyophilized powder, 30-70 units/mg protein

Synonym: GR, NAD(P)H: oxidized-glutathione oxidoreductase

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Properties

form   lyophilized powder
mol wt   mol wt 118 kDa
composition   Protein, ~40% biuret
storage temp.   −20°C

Description

Biochem/physiol Actions

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.

Unit Definition

One unit will reduce 1.0 μmole of oxidized glutathione per min at pH 7.6 at 25°C. (Protein determined by biuret).

Physical form

Lyophilized powder containing trehalose and citrate buffer salts

Price and Availability

Safety & Documentation

Safety Information

WGK Germany 
3

Documents

Certificate of Analysis

Protocols & Articles
Peer-Reviewed Papers
15

References

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