glutathione


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glutathione:

see coenzymecoenzyme
, any one of a group of relatively small organic molecules required for the catalytic function of certain enzymes. A coenzyme may either be attached by covalent bonds to a particular enzyme or exist freely in solution, but in either case it participates intimately in
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.

Glutathione

 

γ-glutamyl cysteinyl glycine, a tripep-tide formed from radicals of three amino acids—glutamic acid, cysteine, and glycine. A peculiarity of the structure of glutathione is the peptide bond between cysteine and glutamic acid, in which the γ-carboxyl of the glutamic acid participates. Glutathione is present in all living organisms and is very important for oxidation-reduction reactions in connection with the capacity of the sulfhydryl group (SH—) of cysteine to undergo the reversible reaction

Glutathione can act as a coenzyme in the action of cathepsins, papain, and other proteolytic enzymes. The function of glutathione in metabolism apparently also includes the protection of the SH group of cytoplasm proteins against oxidation.

glutathione

[¦glüd·ə′thī‚ōn]
(biochemistry)
C10H17O6N3S A widely distributed tripeptide that is important in plant and animal tissue oxidation reactions.
References in periodicals archive ?
Randomized controlled trial of oral glutathione supplementation on body stores of glutathione.
Along with being the crucial antioxidant for the brain, glutathione plays a significant role in detoxification, combining with toxic elements and allowing their excretion from the body.
3]-mediated "oxidative stress" have been difficult to achieve; yet alteration of a defined intracellular redox couple like the glutathione redox pair (GSH/GSSG) would represent an important early indicator of the oxidative effects of [O.
2% lower RBC glutathione concentrations than the control (2.
The role of glutathione and glutathione transferases in chemical carcinogenesis.
In order to measure whole blood glutathione after drawing a blood sample, 500 [micro]L of whole blood was immediately transferred into a tube containing metaphosphoric acid.
As those with some haloalka(e)nes, glutathione conjugates formed such as episulfonium ion (ethylene dibromide) or formaldehyde (dichloromethane) are generally unstable and thus catalyze rather activation reactions (Eaton & Bammler, 1999).
Spectrophotometric quantification of ascorbate (ASC), reduced glutathione (GSH) and vitamin E was performed through the formation of phosphomolybdenum complex.
Chronic stress is another sure-fire way to deplete glutathione.
Glutathione S-transferases (GST) belong to a family of enzymes that is involved in detoxification and toxification mechanisms.

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