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G3664 Sigma

Glutathione Reductase from baker's yeast (S. cerevisiae)

ammonium sulfate suspension, 100-300 units/mg protein (biuret)

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

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Properties

Related Categories 1.6.x.x Acting on NAD or NADP, 1.x.x.x Oxidoreductases, Biochemicals and Reagents, Cell Biology, Cell Signaling and Neuroscience,
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%
storage temp.   2-8°C
Gene Information   bakers yeast ... GLR1(856014)

Description

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

Application

Glutathione Reductase (GR) from baker′s yeast has been used:
• in the glutathione assay to determine glutathione concentration.
• as a standard in the generation of calibration curve.
• as an antigen to measure plasma activity of GR.

Glutathione reductase (GR) from baker′s yeast (Saccharomyces cerevisiae) has been used-
• for quantifying the myocardial tissue glutathione content using a glutathione reductase-5,5′-dithiobis (2-nitrobenzoic acid)-based enzymatic recycling assay
• for the quantification of reduced glutathione (GSH) in the oocytes, using a slightly modified microglutathione assay, obtained from prepubertal gilts
• for the preparation of total GSSG (glutathione disulphide) + GSH measurement, where all available GSSG was reduced to GSH, in rat lens
• for the quantification of intracellular reduced glutathione (GSH) in the oocytes obtained from rats

Biochem/physiol Actions

Glutathione (γ-glutamylcysteinylglycine) is a ubiquitous tripeptide thiol which plays a crucial role in oxidative stress defence mechanism of the cell. Glutathione reductase (GLR1) is responsible for the reduction of the glutathione disulfide (GSSG) to reduced glutathione (GSH).

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.

General description

Glutathione reductase (GLR1) exists in mitochondrial and cytoplasmic isoforms. It shares sequence and structural homology to thioredoxin reductase, and is a flavin-containing oxidoreductase. Its active site is composed of a redox-active disulphide, and it requires NADPH for its catalytic activity. It is a widely present enzyme and is found in plants, bacteria, yeast, mice and humans.

Price and Availability


All labs need water

Biomedical Applications
Safety & Documentation

Safety Information

Symbol 
GHS08  GHS08
Signal word 
Danger
Hazard statements 
Precautionary statements 
RIDADR 
NONH for all modes of transport
WGK Germany 
3
Protocols & Articles

Articles

Ammonium Sulfate Suspensions - Technical Note

Note that for an ammonium sulfate suspension, most of the enzyme will be in solid form. It is likely that only negligible amounts of enzyme will be in the ammonium sulfate solution.
Keywords: Enzyme activity

Related Content

Enzymes & Proteins

Application Index | Enzyme Index | Substrate Index | Inhibitor Index | Cofactor Index | Lectin Index
Keywords: Cell signaling, Diagnostic, Drug discovery, Molecular biology

Peer-Reviewed Papers
15

References

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