Results 301 to 310 of about 487,455 (339)

Inhibition of glutathione peroxidase by coenzyme A

Biochemical and Biophysical Research Communications, 1970
Abstract Glutathione peroxidase has been found to be extremely sensitive to inhibition by coenzyme A. Blocking the SH group of coenzyme A reduces the inhibitory effectiveness about 6-fold. It is thus possible that GSH peroxidase activity is regulated in vivo by the CoA/acyl CoA ratio. Dephospho-CoA was about 11-fold less effective than CoA, and
Radu M. Olinescu, Clive Little, Peter J. O'Brien   +2 more
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Glutathione Peroxidases

2018
Eight glutathione peroxidase (Gpx) genes have been identified in the human and mouse genomes. The conserved redox-active amino acid residue is selenocysteine in five of the human enzymes and cysteine in the others. Cysteine-containing murine Gpx6 is the only difference between mouse and man.
Marcus Conrad, José Pedro Friedmann Angeli   +1 more
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Isolation and purification of glutathione peroxidase

Applied Biochemistry and Microbiology, 2008
Electrophoretically homogeneous glutathione peroxidase (EC 1.11.1.9) preparation from rat liver with a specific activity of 1.46 U/mg of protein and a yield of 7.2% was obtained using the purification procedure developed. The K(M) values for reduced glutathione and hydrogen peroxide were 0.033 and 0.208 mM, respectively.
T. I. Rakhmanova, K. K. Shulgin, T. N. Popova   +2 more
openaire   +3 more sources

Hydrogen Peroxide is Scavenged by Ascorbate-specific Peroxidase in Spinach Chloroplasts

, 1981
Intact spinach chloroplasts scavenge hydrogen peroxide with a peroxidase that uses a photoreductant as the electron donor, but the activity of ruptured chloroplasts is very low [Nakano and Asada (1980) Plant & Cell Physiol. 21: 1295].
Y. Nakano, K. Asada
semanticscholar   +1 more source

Glutathione Peroxidases

2010
Seven glutathione peroxidase (Gpx) genes have been identified in the human and mouse genomes. The conserved redox-active amino acid residue is selenocysteine in most of the enzymes and cysteine in the others. The Gpxs vary in their reaction characteristics and distribution within the organism. Gpx1 is the most abundant and widely distributed Gpx. It is
K.E. Hill, R.F. Burk
openaire   +2 more sources

Reversible near-infrared fluorescent probe introducing tellurium to mimetic glutathione peroxidase for monitoring the redox cycles between peroxynitrite and glutathione in vivo.

Journal of the American Chemical Society, 2013
The redox homeostasis between peroxynitrite and glutathione is closely associated with the physiological and pathological processes, e.g. vascular tissue prolonged relaxation and smooth muscle preparations, attenuation hepatic necrosis, and activation ...
Fabiao Yu, Peng Li, Bingshuai Wang, Keli Han   +3 more
semanticscholar   +1 more source

The Role of Glutathione Peroxidases in Trypanosomatids

Biological Chemistry, 2003
Reactive oxygen species are the unwanted by-products of aerobic metabolism. To protect cells against their potentially lethal effects a series of pathways have evolved that are collectively called the oxidative defence system. In most eukaryotes, catalases and selenium-dependent glutathione peroxidases form the front line of defence against ...
Shane R. Wilkinson, John M. Kelly
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Inactivation of Glutathione Peroxidase by Benzaldehyde

Toxicology and Applied Pharmacology, 1996
Chronic benzaldehyde exposure is known to cause central nervous system (CNS) disturbances. Previous studies have shown that benzaldehyde causes the formation of reactive oxygen species (ROS) in rat synaptosomal fractions. Benzaldehyde has also been implicated in ROS formation in the CNS of rats treated with toluene.
Tahereh Tabatabaie, Robert A. Floyd
openaire   +3 more sources

Oxidation states of glutathione peroxidase

1984
Publisher Summary This chapter discusses a method that has been developed for the reproducible isolation of different oxidized forms of glutathione peroxidase, which can be differentiated by their relative stability and by their reactivity with cyanide.
R.J. Kraus, H.E. Ganther
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GLUTATHIONE PEROXIDASE LEVELS IN BRAIN

Journal of Neurochemistry, 1974
AbstractGlutathione peroxidase activity in brains of various animals was examined. Enzyme activity was low, approximately 10 nmol of glutathione oxidized min−1 mg protein−1 or less. This result suggests that brain tissues contain insufficient glutathione peroxidase activity to provide protection from peroxidative damage and that an alternative ...
Guy M. McKhann, M. Guarnieri, O. de Marchena   +2 more
openaire   +3 more sources