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G6137

Sigma-Aldrich

Glutathione Peroxidase from bovine erythrocytes

lyophilized powder, ≥300 units/mg protein

Synonyme(s) :

GSH-Px, Glutathione:hydrogen-peroxide oxido-reductase

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About This Item

Numéro CAS:
9013-66-5
Numéro de classification (Commission des enzymes):
1.11.1.9 (BRENDA, IUBMB)
Numéro CE :
232-749-6
Numéro MDL:
MFCD00131195
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Source biologique

bovine erythrocytes

Niveau de qualité

200

Forme

lyophilized powder

Activité spécifique

≥300 units/mg protein

Poids mol.

84.5 kDa

Composition

Protein, 10-30% modified Warburg-Christian

Conditions d'expédition

dry ice

Température de stockage

−20°C

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Description générale

Glutathione peroxidase is an antioxidant enzyme that contains selenium. It is present in the glandular epithelium of human endometrium.

Application

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.
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.

Actions biochimiques/physiologiques

Glutathione peroxidase helps to reduce (peroxides) H2O2 to water and lipid peroxides to lipid alcohols.
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.
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.

Définition de l'unité

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.

Forme physique

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

Autres remarques

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.

Produit(s) apparenté(s)

Réf. du produit
Description
Tarif

Pictogrammes

Health hazard
GHS08

Mention d'avertissement

Danger

Mentions de danger

H334

Conseils de prudence

P261 - P284 - P501

Classification des risques

Resp. Sens. 1

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)

Certificats d'analyse (COA)

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Reactive oxygen species, oxidative stress, and vascular biology in hypertension
Comprehensive hypertension, 337-344 (2007)
Yue Wang et al.
Analytical chemistry, 92(2), 1997-2004 (2019-12-21)
Solid evidence confirms that glutathione peroxidase (GPx) is a kind of vital protease in the first-line antioxidant defense system and participates in regulation of redox homeostasis as well as the pentose phosphate pathway. However, the current methods cannot achieve real-time
J T Jones et al.
Gene, 324, 47-54 (2003-12-25)
We report the cloning and characterisation of full-length DNAs complementary to RNA (cDNAs) encoding two glutathione peroxidases (GpXs) from a plant parasitic nematode, the potato cyst nematode (PCN) Globodera rostochiensis. One protein has a functional signal peptide that targets the
The role of oxidative stress in endometriosis
Handbook of Fertility, 273-281 (2015)
Hemoglobin catabolism. I. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidative breakdown.
G C MILLS
The Journal of biological chemistry, 229(1), 189-197 (1957-11-01)
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