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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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The following article is from The Great Soviet Encyclopedia (1979). It might be outdated or ideologically biased.



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.

The Great Soviet Encyclopedia, 3rd Edition (1970-1979). © 2010 The Gale Group, Inc. All rights reserved.


C10H17O6N3S A widely distributed tripeptide that is important in plant and animal tissue oxidation reactions.
McGraw-Hill Dictionary of Scientific & Technical Terms, 6E, Copyright © 2003 by The McGraw-Hill Companies, Inc.
References in periodicals archive ?
* Promotes healthy aging by contributing to the body's antioxidant defenses and GSH levels that naturally decline with age.
All in all, the toxicity induced by PZA was accompanied by increased ROS formation, lipid peroxidation, GSH depletion, and induction of apoptosis.
In pig, the paternal chromosomal integrity of sperm treated with DTT was compromised compared to GSH treated sperm.
It was further observed that the AuNCs-BSA solution containing [Cu.sup.2+] emitted strong fluorescence again after treatment with of 1.6 mM GSH (Figure 1).
On the basis of the observed mass spectrometric data, we propose that M2 and M2' are generated by intramolecular cyclization after GSH was conjugated to the cis-enedial intermediate which was derived from LIM.
o-Phthaldialdehyde (OPA, 99%), sodium hydroxide (NaOH, 97%), methanol (MeOH, 99%), 2-propanol (2-PRO, 99.5%), ethanol (EtOH, abs), l-glutathione reduced (GSH, >98%), l-homocysteine (HCY, [greater than or equal to]98%), l-cysteine (CYS, 97%), magnesium nitrate hexahydrate [(Mg(N[O.sub.3]).sub.2] x 6[H.sub.2]O, puriss p.a.), calcium carbonate (CaC[O.sub.3], 98%), citric acid ([C.sub.6][H.sub.8][O.sub.7], 99%), and zinc chloride (Zn[Cl.sub.2], puriss p.a.) were obtained from Sigma-Aldrich.
Este tripetido ([gamma]-glutamilcisteinilglicina) sintetizado en el citosol de las celulas, con propiedades reductoras y nucleofilas, cumple diversas funciones, entre ellas la homeostasis redox, lo cual reduce el dano oxidativo intracelular con un papel importante en las bacterias como factor protector contra el EO generado en el huesped, la resistencia bacteriana a la accion del [H.sub.2][O.sub.2] dependeria de la acumulacion de GSH, que puede activar en las celulas el sistema GSH-glutation peroxidasa /glutation reductasa (14) .
The mean GSH levels obtained from lenses in the control, sham, and sesamol groups were 13[+ or -]0.90, 6.0[+ or -]0.15, and 12[+ or -]0.93 [micro]mol/L, respectively.
GSH treatment 30 minutes before reperfusion was associated with a significant increase in the withdrawal thresholds of both hind paws following reperfusion.
The key enzyme that mediates the recycling of GSH is the glutathione reductase (GSR), a homodimeric flavoprotein that catalyzes GSSG reduction to GSH by using NADPH as a reducing cofactor.
The cleavage reaction occurs immediately in the short time due to the high concentration of glutathione (GSH).