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Key Documents

G3664

Sigma-Aldrich

Glutathione Reductase from baker′s yeast (S. cerevisiae)

ammonium sulfate suspension, 100-300 units/mg protein (biuret)

동의어(들):

GR, NAD(P)H:oxidized-glutathione oxidoreductase

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About This Item

CAS Number:
효소 위원회 번호:
MDL number:
UNSPSC 코드:
12352204
NACRES:
NA.47

형태

ammonium sulfate suspension

Quality Level

특이 활성도

100-300 units/mg protein (biuret)

분자량

118 kDa

UniProt 수납 번호

외래 활성

G-6-PDH, 6-PGDH, and NADPH oxidase ≤0.01%
lipoamide dehydrogenase ≤0.1%

저장 온도

2-8°C

유전자 정보

bakers yeast ... GLR1(856014)

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일반 설명

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.

애플리케이션

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

생화학적/생리학적 작용

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.

단위 정의

One unit will reduce 1.0 μmole of oxidized glutathione per min at pH 7.6 at 25 °C.

물리적 형태

Suspension in 3.6 M (NH4)2SO4, pH 7.0, containing 0.1 mM dithiothreitol

제조 메모

Purified by affinity chromatography

억제제

제품 번호
설명
가격

픽토그램

Health hazard

신호어

Danger

유해 및 위험 성명서

예방조치 성명서

Hazard Classifications

Resp. Sens. 1

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 2

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable


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문서 라이브러리에서 최근에 구매한 제품에 대한 문서를 찾아보세요.

문서 라이브러리 방문

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
Tünde Pusztahelyi et al.
Journal of trace elements in medicine and biology : organ of the Society for Minerals and Trace Elements (GMS), 30, 96-101 (2014-12-20)
Selenium deficiency is a major health problem worldwide for about 1 billion people. Bacterial cells usually possess low tolerance to selenite stress and also low ability to reduce high concentrations of toxic selenite. Here, high tolerance to selenite and selenium
Yan-Guang Wu et al.
Cell research, 17(8), 722-731 (2007-08-08)
Selecting oocytes that are most likely to develop is crucial for in vitro fertilization and animal cloning. Brilliant cresyl blue (BCB) staining has been used for oocyte selection in large animals, but its wider utility needs further evaluation. Mouse oocytes
Jing Wang et al.
Acta ophthalmologica, 88(7), 779-785 (2010-01-28)
To investigate the evolution of cataract development and glutathione redox balance in the rat lens after in vivo close-to-threshold dose exposure to ultraviolet radiation (UVR) around 300 nm. Three groups of 10 Sprague-Dawley rats were unilaterally exposed to 8 kJ/m²

문서

Instructions for working with enzymes supplied as ammonium sulfate suspensions

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