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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 Columbia Electronic Encyclopedia™ Copyright © 2013, Columbia University Press. Licensed from Columbia University Press. All rights reserved.
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 It might be outdated or ideologically biased.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 ?
For example, reduced glutathione (GSH) levels change from 71% of the reference (normal) value before therapy to 93% of reference value after 6 months of therapy, and SAM values change from 89.7% of reference value to 98% of reference value at 6 months.
However, curcumin treatment has restored the reduced glutathione level in the brain tissues of PTZ-kindled mice.
It is our view that the present measurements of reduced glutathione in the blood plasma are more indicative of the reduced glutathione levels in the cells of interest in CFS than are the measurements reported in the literature, for these reasons.
Glutathione peroxidase activity (Gpx) (a), glutathione reductase activity (GR) (b), reduced glutathione (GSH) (c), and glucose6-phosphate dehydrogenase activity (G6PDH) (d).
S-acetylglutathione is able to increase intracellular-SH groups as reported by Vogel et al., is more stable in blood plasma than GSH, and enters the cells directly, where it is converted to reduced glutathione by the abundant cytoplasm thioesterases.
The assay system contained 2.2 ml of phosphate buffer (50 mM, pH 7.0), 0.1 ml EDTA (1.5 mM) 0.1 ml sodium azide (1 mm), 0.1 ml reduced glutathione (1 mM), 0.1 ml NADPH (0.2 mM), 0.1 ml glutathione reductase (1 U/ml) and sutable amount of lysate to make the volume up to 2.8 ml.
(3) Nonstandard abbreviations: GSH, reduced glutathione; LC/ESI-MS, liquid chromatography/electrospray ionization-mass spectrometry; Hb, hemoglobin; and metHb, methemoglobin.
The procedure to estimate the reduced glutathione (GSH) level followed the method described by Ellman [14].
GSSH-Red regenerates reduced glutathione (GSH) from oxidized glutathione, which has been formed by oxidation while CAT is responsible for the scavenging or detoxification of [H.sub.2][O.sub.2].
Reduced glutathione and total glutathione were higher in the epidermis than in the dermis by 513 and 471%.
The CEH-CDH method for determining serum cholesterol has several advantages over traditional methods: rapidity, simplicity, and no interference from various reductants, bilirubin, ascorbic acid, or reduced glutathione. Moreover, because the amount of [beta]-NADH formed is equivalent to the amount of cholesterol, the concentration of cholesterol in serum can be estimated from a factor calculated from the measured molar absorptivity of [beta]-NADH calibrated by that in the Standard Reference Material.
Glutathione reductase (GSH-R, EC is a flavoprotein that catalyzes the NADPH-dependent reduction of oxidized glutathione (GSSG) to reduced glutathione (GSH).

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