G3664
Glutathione Reductase from baker′s yeast (S. cerevisiae)
ammonium sulfate suspension, 100-300 units/mg protein (biuret)
Synonyme(s) :
GR, NAD(P)H:oxidized-glutathione oxidoreductase
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About This Item
Numéro CAS:
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.47
Produits recommandés
Forme
ammonium sulfate suspension
Activité spécifique
100-300 units/mg protein (biuret)
Poids mol.
118 kDa
Numéro d'accès UniProt
Activité étrangère
G-6-PDH, 6-PGDH, and NADPH oxidase ≤0.01%
lipoamide dehydrogenase ≤0.1%
Température de stockage
2-8°C
Informations sur le gène
bakers yeast ... GLR1(856014)
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Description générale
Glutathione reductase (GLR1) exists in mitochondrial and cytoplasmic isoforms. It shares sequence and structural homology to thioredoxin reductase, and is a flavin-containing oxidoreductase. Its active site is composed of a redox-active disulphide, and it requires NADPH for its catalytic activity. It is a widely present enzyme and is found in plants, bacteria, yeast, mice and humans.
Application
Glutathione Reductase (GR) from baker′s yeast has been used:
- in the glutathione assay to determine glutathione concentration.
- as a standard in the generation of calibration curve.
- as an antigen to measure plasma activity of GR.
Glutathione reductase (GR) from baker′s yeast (Saccharomyces cerevisiae) has been used-
- for quantifying the myocardial tissue glutathione content using a glutathione reductase-5,5′-dithiobis (2-nitrobenzoic acid)-based enzymatic recycling assay
- for the quantification of reduced glutathione (GSH) in the oocytes, using a slightly modified microglutathione assay, obtained from prepubertal gilts
- for the preparation of total GSSG (glutathione disulphide) + GSH measurement, where all available GSSG was reduced to GSH, in rat lens
- for the quantification of intracellular reduced glutathione (GSH) in the oocytes obtained from rats
Actions biochimiques/physiologiques
Glutathione (γ-glutamylcysteinylglycine) is a ubiquitous tripeptide thiol which plays a crucial role in oxidative stress defence mechanism of the cell. Glutathione reductase (GLR1) is responsible for the reduction of the glutathione disulfide (GSSG) to reduced glutathione (GSH).
Glutathione reductase IGR) is a crucial flavoenzyme in the antioxidant defense system. Reduced glutathione (GSH) is used by glutathione peroxidase to detoxify hydrogen peroxide and in the process is converted to oxidized glutathione (GSSG). The GSSG is then recycled back to GSH by glutathione reductase (GR) using NADPH that is then converted to NADP+. The regenerated GSH is then available to detoxify more hydrogen peroxide. The enzyme uses FAD as a cofactor. GR and glutathione peroxidase may inhibit lipid peroxidation by functioning as antioxidant enzymes in sperm. Glutathione reductase shares a structural motif with a number of other proteins including aspartyl proteases, citrate synthase, EF hands, hemoglobins, lipocalins, and α/β hydrolases. GR is stimulated by melatonin and is reportedly irreversibly inhibited by a number of oxygen radical generating systems.
Définition de l'unité
One unit will reduce 1.0 μmole of oxidized glutathione per min at pH 7.6 at 25 °C.
Forme physique
Suspension in 3.6 M (NH4)2SO4, pH 7.0, containing 0.1 mM dithiothreitol
Notes préparatoires
Purified by affinity chromatography
Inhibiteur
Réf. du produit
Description
Tarif
Produit(s) apparenté(s)
Mention d'avertissement
Danger
Mentions de danger
Conseils de prudence
Classification des risques
Resp. Sens. 1
Code de la classe de stockage
12 - Non Combustible Liquids
Classe de danger pour l'eau (WGK)
WGK 2
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
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Les clients ont également consulté
Feng Gao et al.
The Journal of pharmacology and experimental therapeutics, 301(2), 543-550 (2002-04-19)
The present experiment determined the effects of glutathione and ascorbic acid, the two most important hydrophilic antioxidants, on myocardial ischemia-reperfusion injury and evaluated their relative therapeutic values. Isolated rat hearts were subjected to ischemia (30 min) and reperfusion (120 min)
Caryn E Outten et al.
The Journal of biological chemistry, 279(9), 7785-7791 (2003-12-16)
To combat oxidative damage, eukaryotic cells have evolved with numerous anti-oxidant factors that are often distributed between cytosolic and mitochondrial pools. Glutathione reductase, which regenerates the reduced form of glutathione, represents one such anti-oxidant factor, yet nothing is known regarding
Kristin K Brown et al.
Free radical biology & medicine, 45(4), 494-502 (2008-05-27)
Isothiocyanates are phytochemicals with anti-cancer properties that include the ability to trigger apoptosis. A substantial body of evidence suggests that reaction of the electrophilic isothiocyanate moiety with cysteine residues in cellular proteins and glutathione accounts for their biological activity. In
I P Gontar et al.
Bulletin of experimental biology and medicine, 150(6), 765-769 (2012-01-12)
The proposed method of emulsive polymerization provides the possibility of modifying and obtaining insoluble forms of superoxide dismutase (SOD), glutathione reductase, and streptolysin-O preserving nanoobjects (conformationally active centers and antigenic determinants) in their native states. Apart from enzymatic and immunological
Eugine Lee et al.
Reproduction (Cambridge, England), 134(3), 405-414 (2007-08-22)
In an effort to improve the quality of in vitro produced porcine embryos, we investigated the effect of brain-derived neurotropic factor (BDNF), a neurotropin family member, on in vitro maturation (IVM) of porcine oocytes. The expression of BDNF and truncated
Articles
Instructions for working with enzymes supplied as ammonium sulfate suspensions
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