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Merck

G6137

Sigma-Aldrich

Glutathione Peroxidase from bovine erythrocytes

lyophilized powder, ≥300 units/mg protein

Synonim(y):

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

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About This Item

Numer CAS:
Numer EC enzymu:
Numer WE:
Numer MDL:
Kod UNSPSC:
12352204
NACRES:
NA.54

pochodzenie biologiczne

bovine erythrocytes

Poziom jakości

Formularz

lyophilized powder

aktywność właściwa

≥300 units/mg protein

masa cząsteczkowa

84.5 kDa

skład

Protein, 10-30% modified Warburg-Christian

Warunki transportu

dry ice

temp. przechowywania

−20°C

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Opis ogólny

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

Zastosowanie

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.

Działania biochem./fizjol.

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.

Definicja jednostki

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.

Postać fizyczna

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

Inne uwagi

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.
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Piktogramy

Health hazard

Hasło ostrzegawcze

Danger

Zwroty wskazujące rodzaj zagrożenia

Zwroty wskazujące środki ostrożności

Klasyfikacja zagrożeń

Resp. Sens. 1

Kod klasy składowania

11 - Combustible Solids

Klasa zagrożenia wodnego (WGK)

WGK 3

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable

Środki ochrony indywidualnej

Eyeshields, Gloves, type N95 (US)


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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

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

Produkty

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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