Results 281 to 290 of about 487,455 (339)

Assays of glutathione peroxidase.

Methods in Enzymology, 1984
Publisher Summary To determine glutathione peroxidase reliably, some factors of potential pitfall have to be considered, for example, enzymatic side reactions of substrates (especially when crude tissue samples are assayed), high and variable spontaneous reaction rates of substrates, and the peculiar kinetics of the enzyme itself.
L. Flohé, W. Günzler
semanticscholar   +3 more sources

Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase.

Journal of Laboratory and Clinical Medicine, 1967
An assay procedure is described in which blood cell glutathione peroxidase may be accurately measured by a direct spectrophotometric procedure. Glutathione peroxidase activity is found to be associated with a relatively stable, nondialyzable, heat-labile,
D. Paglia, W. N. Valentine
semanticscholar   +1 more source

Glutathione peroxidases

Biochimica et Biophysica Acta (BBA) - General Subjects, 2013
With increasing evidence that hydroperoxides are not only toxic but rather exert essential physiological functions, also hydroperoxide removing enzymes have to be re-viewed. In mammals, the peroxidases inter alia comprise the 8 glutathione peroxidases (GPx1-GPx8) so far identified.Since GPxs have recently been reviewed under various aspects, we here ...
Brigelius Flohé R, MAIORINO, MATILDE
openaire   +2 more sources

Erythrocyte Glutathione Peroxidase

Encyclopedia of Autism Spectrum Disorders, 2018
J. Kopel
semanticscholar   +2 more sources

Kinetics of glutathione peroxidase

Biochimica et Biophysica Acta (BBA) - Enzymology, 1969
Abstract The dependency of the reaction rate of purified glutathione peroxidase (GSH: H2O2 oxidoreductase, EC 1.11.1.9) on the concentration of the substrates is investigated employing methods by which the substrates involved are determined immediately. GSH is measured polarographically. H2O2 is estimated by enzymatic oxidation of the fluorescent dye
Leopold Flohé, Ingeborg Brand
openaire   +3 more sources

Gastrointestinal glutathione peroxidase

BioFactors, 1999
AbstractThe gastrointestinal glutathione peroxidase (GI‐GPx) is the fourth member of the GPx family. In rodents, it is exclusively expressed in the gastrointestinal tract, in humans also in liver. It has, therefore, been discussed to function as a primary barrier against the absorption of ingested hydroperoxides.
Kirstin Wingler, Regina Brigelius-Flohé
openaire   +3 more sources

[47] Phospholipid hydroperoxide glutathione peroxidase

Phosphorus and Sulfur and the Related Elements, 1988
In acute inflammation the activated leukocytes generate cytotoxic oxygen free radicals. The role of these radical species in the cellular damage following an acute inflammatory reaction is well known. On the other hand the extent of the cellular damage must be dependent on both the rate of the free-radical generation and the scavenging capacity of the ...
MAIORINO, MATILDE, ROVERI, ANTONELLA, URSINI, FULVIO   +2 more
openaire   +8 more sources

The Catalytic Site of Glutathione Peroxidases

Antioxidants & Redox Signaling, 2008
In GPxs, the redox-active Se or S, is at hydrogen bonding distance from Gln and Trp residues that contribute to catalysis. From sequence homology of >400 sequences and modeling of the DmGPx as a paradigm, Asn136 emerged as a fourth essential component of the active site.
TOSATTO, SILVIO, BOSELLO TRAVAIN, VALENTINA, F. FOGOLARI, P. MAURI, ROVERI, ANTONELLA, TOPPO, STEFANO, L. FLOHE L, URSINI, FULVIO, MAIORINO, MATILDE   +8 more
openaire   +7 more sources

Selenium: biochemical role as a component of glutathione peroxidase.

Science, 2009
When hemolyzates from erythrocytes of selenium-deficient rats were incubated in vitro in the presence of ascorbate or H(2)O(2), added glutathione failed to protect the hemoglobin from oxidative damage.
J. T. Rotruck, A. L. Pope, H. Ganther, A. Swanson, D. Hafeman, W. Hoekstra   +5 more
semanticscholar   +1 more source