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G6137

Sigma-Aldrich

Glutathion-Peroxidase aus Rindererythrocyten

lyophilized powder, ≥300 units/mg protein

Synonym(e):

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

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About This Item

CAS-Nummer:
9013-66-5
EC-Nummer:
1.11.1.9 (BRENDA, IUBMB)
EG-Nummer:
232-749-6
MDL-Nummer:
MFCD00131195
UNSPSC-Code:
12352204
NACRES:
NA.54

Biologische Quelle

bovine erythrocytes

Qualitätsniveau

200

Form

lyophilized powder

Spezifische Aktivität

≥300 units/mg protein

Mol-Gew.

84.5 kDa

Zusammensetzung

Protein, 10-30% modified Warburg-Christian

Versandbedingung

dry ice

Lagertemp.

−20°C

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Allgemeine Beschreibung

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

Anwendung

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.

Biochem./physiol. Wirkung

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.

Einheitendefinition

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.

Physikalische Form

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

Sonstige Hinweise

Anm.: Beim angegebenen optimalen pH von 8.8 stellten wir eine 10 Mal höhere Aktivität als beim pH von 7.0 fest. Um im Einklang mit der Literatur zu bleiben und Komplikationen aus der nicht-enzymatischen Oxidation von GSH zu umgehen, definieren wir unsere Einheit bei pH 7.0.

Piktogramme

Health hazard
GHS08

Signalwort

Danger

H-Sätze

H334

Gefahreneinstufungen

Resp. Sens. 1

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, type N95 (US)

Analysenzertifikate (COA)

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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
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)
O Werz et al.
European journal of biochemistry, 242(1), 90-97 (1996-11-15)
Differentiation of HL-60 cells by dimethylsulfoxide induces 5-lipoxygenase protein expression, but only low cellular 5-lipoxygenase activity. Similarly, B-lymphocytes express 5-lipoxygenase protein and show activity in cell homogenates but not in intact cells. Here, we demonstrate that suppression of cellular 5-lipoxygenase
The role of oxidative stress in endometriosis
Handbook of Fertility, 273-281 (2015)
Angeles Torres et al.
Die Nahrung, 47(6), 430-433 (2004-01-20)
An analytical method for determining glutathione peroxidase (GPx) (EC 1.11.1.9) activity in whole blood has been adapted to human milk samples. The values obtained for precision (relative standard deviation: 8.4%), linearity and accuracy (recovery: 90.4%) indicate the adequacy of the
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