glutathione


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glutathione

 [gloo″tah-thi´ōn]
a tripeptide of glutamic acid, cysteine, and glycine; the reduced form (GSH) serves as a reducing agent in many biochemical reactions, being converted to oxidized glutathione (GSSG) in which the cysteine residues of two glutathione molecules are connected by a disulfide bridge. Reduced glutathione is important in protecting erythrocytes from oxidation and hemolysis; deficiency causes sensitivity to oxidant drugs.

glu·ta·thi·one (GSH),

(glū'tă-thī'ōn),
A tripeptide of glycine, l-cysteine, and l-glutamate, with l-glutamate having an isopeptide bond with the amino moiety of l-cysteine. Glutathione has a wide variety of roles in a cell; it is the most prevalent non-protein thiol. Glutathione disulfide (GSSG) consists of two glutathiones linked through a disulfide bridge; the term oxidized glutathione for GSSG should be avoided because it includes the sulfones and sulfoxides. (The term reduced glutathione is not necessary because glutathione is the thiol form.) A deficiency of glutathione can cause hemolysis with oxidative stress. It is also used in the course of intermediary metabolism as a donor of thiol (SH) groups and is essential for detoxification of acetaminophen.
See also: oxidized glutathione, reduced glutathione, glutathione reductase.

glutathione

/glu·ta·thi·one/ (gloo″tah-thi´ōn) a tripeptide of glutamic acid, cysteine, and glycine, existing in reduced (GSH) and oxidized (GSSG) forms and functioning in various redox reactions: in the destruction of peroxides and free radicals, as a cofactor for enzymes, and in the detoxification of harmful compounds. It is also involved in the formation and maintenance of disulfide bonds in proteins and in transport of amino acids across cell membranes.

glutathione

(glo͞o′tə-thī′ōn′)
n.
A tripeptide, C10H17N3O6S, of glycine, cysteine, and glutamic acid that occurs widely in plant and animal tissues and is important in biological oxidation-reduction reactions.

glutathione

[glo̅o̅′təthī′ōn]
Etymology: L, gluten + Gk, theione, sulfur
a tripeptide of glutamic acid, cysteine, and glycine whose deficiency is commonly associated with hemolytic anemia. It functions by taking up and giving off hydrogen. It transports amino acids across cell membranes and conjugates to drugs enabling excretion.

glutathione

A ubiquitous tripeptide with antioxidant activity involved in CNS metabolism, serving as a coenzyme for some enzymes of oxidation-reduction systems, transmembrane amino acid transport, maintenance of red cell integrity and prevention of H2O2 accumulation in red cells.
 
Glutathione-rich foods
Asparagus, avocado, broccoli, oranges, squash, strawberries and watermelon.

glutathione

γ-Glutamyl-cysteinyl-glycine A ubiquitous antioxidant tripeptide involved in CNS metabolism, which serves as a coenzyme for some enzymes of oxidation-reduction systems, transmembrane amino acid transport, maintaining RBC integrity, and prevention of H2O2 accumulation in RBCs. See Antioxidant, Antioxidant therapy, Free radical, Free radical scavenger.

glu·ta·thi·one

(GSH) (glū'tă-thī'ōn)
1. The principal low molecular weight thiol compound of living plant cells; used in the course of intermediary metabolism as a donor of thiol (SH) groups; essential for detoxification of acetaminophen.
2. Compound has a wide variety of roles in a cell. A deficiency can cause hemolysis with oxidative stress.

glutathione

A tripeptide amino acid derivative that protects red cells from oxidative damage and, in the form of the enzyme glutathione peroxidase, plays an important role in detoxifying hydrogen peroxide and organic peroxides produced in the body. Glutathione also participates in the transport of amino acids from one cell to another.

Glutathione

A molecule that acts as a co-enzyme in cellular oxidation-reduction reactions.

glutathione (glōō·t·thīˑ·ōn),

n a tripeptide that comprises cysteine, glutamic acid, and glycine. An important antioxidant, instrumental in the glutathione conjugation detoxifica-tion pathway. See also glutathione conjugation.

glu·ta·thi·one

(glū'tă-thī'ōn)
A tripeptide of glycine, l-cysteine, and l-glutamate; essential for detoxification of acetaminophen.

glutathione (gloo´təthī´ōn),

n an enzyme whose deficiency is commonly associated with hemolytic anemia.

glutathione

reduced glutathione (GSH), a tripeptide containing glutamic acid, cysteine and glycine, which serves as a reducing agent in many biochemical reactions, being converted to oxidized glutathione (GSSG) in which the cysteine residues of two glutathione molecules are connected by a disulfide bridge. Reduced glutathione is important in protecting erythrocytes from oxidation and hemolysis; deficiency causes sensitivity to oxidant drugs.

glutathione peroxidase
a selenium-containing enzyme whose blood level is a good indicator of the selenium status of the animal; occurs in a plasma form, an enzyme with specificity for phospholipids, and an intracellular form. Called also GPx.
glutathione reductase
a flavin enzyme involved in the defense of the erythrocyte against hemolysis. A partial deficiency occurs relatively frequently but is due to a deficiency of riboflavin; called also GR.
References in periodicals archive ?
The gross conformation and key residues involved in the interaction between glutathione sulfonate and GST pi are very similar to the 3D structure of the mu class GST complexed with reduced glutathione (Ji et al.
The study found that pretreatment with NAC raised glutathione in older cells and helped offset cell death.
What accounts for this study is the function and responsibility of the 2 enzymes: glutathione reductase and catalase which are essential for many physiological responses of the body (7).
1 Glutathione is a new tool in the cosmetic industry.
Pharmacokinetics of glutathione and its metabolites in normal subjects.
Hepatic glutathione content in patients with alcoholic and non alcoholic liver disease.
After years of research and clinical study, he discovered a newer, safer, and more effective way for the body to absorb and use glutathione.
To identify glutathione molecules bonded with cysteine residues, we searched the cavities with unresolved electron density.
This sharp decrease in GSH could be explained by a reaction/direct connection fungicide with glutathione, indeed the carboxyl groups of glutathione (amine group, sulfhydryl group (-GH) and two peptides) are combined with the fungicide [13].
Glutathione (-glutamyl-l-cystinylglycine) is a non-protein thiol, widely distributed in animal tissues, plants and microorganisms.
Normally, when nitric oxide reacts with superoxide, superoxide dismutase (SOD) corrals the free radical and converts it to hydrogen peroxide, which is then further converted to water and molecular oxygen by catalase and glutathione peroxidase.
When these phenolic compounds are oxidized pre-fermentation, the quinones that are formed can be eliminated by the glutathione thiol naturally present in grape juice.

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