glutathione reductase


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glu·ta·thi·one re·duc·tase

[MIM*138300]
an enzyme that catalyzes the reaction of glutathione disulfide with NADH (or NADPH), forming two glutathiones and NAD+ (or NADP+); involved in many redox reactions; a deficiency can cause hemolysis with oxidative stress.
References in periodicals archive ?
(c) Glutathione reductase activity: controls versus ATV: p = 0.038; controls versus ATV + vitEC: p = 0.008.
Spooner, "Glutathione reductase. NAD(P)H: oxidized Glutathione oxidoreductase," in Methods of Enzymatic Analysis, H.
Novoselov et al., "Platyhelminth mitochondrial and cytosolic redox homeostasis is controlled by a single thioredoxin glutathione reductase and dependent on selenium and glutathione," The Journal of Biological Chemistry, vol.
Several factors have made this study important and they are as follow: lack of such studies in the country and the ambiguity in the condition of glutathione reductase and catalase after different training methods, especially in females' sports.
Reduced status of antioxidants such as glutathione and ascorbic acid is maintained by glutathione reductase (GR), monodehydroascorbate reductase (MDAR) and dehydroascorbate reductase (DHAR), using NADPH as areducing agent (Apel and Hirt, 2004; Bhattacharjee, 2005; Gill andTuteja, 2010).
From table (2), the activity of glutathione reductase (GR) was extremely significantly decreased in C[Cl.sub.4], C[Cl.sub.4] & NSO and protective groups (P<0.001), compared with normal control group (P<0.05).
The query asking glutathione reductase gene from CyanoBase (The Genome Database for Cyanobacteria) for the reference strain Synechocystis sp.
The supernatant obtained were maintained in an ice bath and used for the estimation of total protein, lipid peroxidation, glutathione reductase, reduced glutathione, glutathione peroxidase and superoxide dismutase.
Glutathione reacts rapidly and needs to be exposed inside the yeast cell to enzyme glutathione reductase to be reactivated.
The product of glutathione oxidation, oxidized glutathione, is known to be toxic and is rapidly converted back to glutathione by the enzyme glutathione reductase (Cotran et al., 1989).
Glutathione peroxidase (GPX) and glutathione reductase enzyme action is related to glutathione reduction and oxidation (Bakalli et al., 1995).
GSH-dependent detoxification involves glutathione peroxidase (GSHx), which has a pivotal role in the elimination of hydrogen and organic peroxides and leads to the formation of oxidized glutathione but is reduced back to its thiol form (GSH) by glutathione reductase (GSHr), leading to the consumption of NADPH, which is chiefly formed by pentose phosphate pathway.

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