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G6137

Sigma-Aldrich

Glutathione Peroxidase from bovine erythrocytes

lyophilized powder, ≥300 units/mg protein

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Synonym(s):
GSH-Px, Glutathione:hydrogen-peroxide oxido-reductase
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
NACRES:
NA.54

biological source

bovine erythrocytes

Quality Level

form

lyophilized powder

specific activity

≥300 units/mg protein

mol wt

84.5 kDa

composition

Protein, 10-30% modified Warburg-Christian

shipped in

dry ice

storage temp.

−20°C

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This Item
S5395S7446S7571
biological source

bovine erythrocytes

biological source

bovine erythrocytes

biological source

-

biological source

bovine

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

shipped in

dry ice

shipped in

dry ice

shipped in

-

shipped in

-

mol wt

84.5 kDa

mol wt

32.5 kDa

mol wt

32.5 kDa

mol wt

32.5 kDa

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

General description

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.

Biochem/physiol Actions

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.

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.

Physical form

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

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.

related product

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Customers Also Viewed

Slide 1 of 2

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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
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)
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
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

Articles

Oxidative stress is mediated, in part, by reactive oxygen species produced by multiple cellular processes and controlled by cellular antioxidant mechanisms such as enzymatic scavengers or antioxidant modulators. Free radicals, such as reactive oxygen species, cause cellular damage via cellular.

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