Not available outside of the UK & Ireland.

Application

Glutathione peroxidase from bovine erythrocytes was used as a positive control in cloning and characterization of full-length cDNAs encoding two glutathione peroxidases (GpXs) from Globodera rostochiensis. It was used for the determination of glutathione peroxidase activity in human milk.

Glutathione Peroxidase from bovine erythrocytes has been used as an oxygen radical scavenger to study its effect on cytotoxicity of 1,3-dilinoleoylglycerol (DLG) against E1A-3Y1 cells.

Biochem/physiol Actions

Protects cells against oxidative damage by catalyzing the reduction of hydrogen peroxide in the presence of reducing agent glutathione. In cellular membranes it may induce lipid peroxidation through the reduction of hydrogen peroxide or polyunsaturated fatty acid hydroperoxides.

Glutathione peroxidase is an enzyme which reduced lipid hydroperoxides into their corresponding alcohols. It also reduces free hydrogen peroxide in to water. In vivo it is responsible for protecting hemoglobin from oxidative breakdown.

Glutathione peroxidase helps to reduce (peroxides) H₂O₂to water and lipidperoxidesto lipid alcohols.

General description

Glutathione peroxidaseis an antioxidant enzyme that contains selenium. It is present in the glandular epithelium of humanendometrium.

Other Notes

Note: At the reported pH optimum of 8.8, we have found the activity to be approx. 10 times that at pH 7.0. However, to remain consistent with literature and avoid complications arising from non-enzymatic oxidation of GSH, our unit is defined at pH 7.0.

Packaging

100, 200, 500 units in serum bottle

Physical form

Lyophilized powder containing 25% sucrose and 2.5% dithiothreitol with sodium phosphate buffer salts

Unit Definition

One unit will catalyze the oxidation by H₂O₂ of 1.0 µmole of reduced glutathione to oxidized glutathione per min at pH 7.0 at 25 °C.