Results 111 to 120 of about 167,145 (165)

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.
K K, Shul'gim, T N, Popova, T I, Rakhmanova   +2 more
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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
C, Little, R M, Olinescu, P J, O'Brien
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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 ...
O, De Marchena, M, Guarnieri, G, McKhann
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Reaction of cyanide with glutathione peroxidase

Biochemical and Biophysical Research Communications, 1980
An oxidized form of ovine erythrocyte GSH peroxidase (Form C) that contains bound glutathione in equimolar ratio to the enzyme selenium is inactivated by cyanide. When Form C was treated with 1 or 10 mM KCN at pH 7.5, there was a rapid increase in ultraviolet absorption at 250 nm, S-cyanoglutathione was released, and the enzyme was reduced, as shown by
R J, Kraus, H E, Ganther
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Selenoglutaredoxin as a Glutathione Peroxidase Mimic

ChemBioChem, 2008
AbstractGlutaredoxin (Grx1) from Escherichia coli is a monomeric, 85‐amino‐acid‐long, disulfide‐containing redox protein. A Grx1 variant in which the redox‐active disulfide was replaced with a selenocysteine (C11U/C14S) was prepared by native chemical ligation from three fragments as a potential mimic of the natural selenoenzyme glutathione peroxidase (
Casi G, Roelfes G, Hilvert D
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Erythrocyte Glutathione‐Peroxidase Deficiency

British Journal of Haematology, 1970
Summary Glutathione peroxidase deficiency is the most recently described erythrocyte enzyme abnormality. This enzyme occupies a critical position in the pathways leading to the decomposition of peroxides in the erythrocyte. On the basis of our studies of patients with GSH‐P deficiency, it appears that a spectrum of disease quite similar to that found ...
T F, Necheles, M H, Steinberg, D, Cameron   +2 more
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Homocysteine and Glutathione Peroxidase-1

Antioxidants & Redox Signaling, 2007
Mildly elevated homocysteine levels (Hcy) increase the risk for atherothrombotic vascular disease in the coronary, cerebrovascular, and peripheral arterial circulations. The molecular mechanisms responsible for decreased bioavailability of endothelium-derived nitric oxide (NO) by Hcy involve an increase of vascular oxidant stress and inhibition of ...
Edith, Lubos, Joseph, Loscalzo, Diane E, Handy   +2 more
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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.
H E, Ganther, R J, Kraus
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Inactivation of Glutathione Peroxidase by Peroxynitrite

Archives of Biochemistry and Biophysics, 1998
Glutathione peroxidase (GSH-Px) is inactivated on exposure to peroxynitrite under physiologically relevant conditions. Stopped-flow kinetic studies show that the reaction between peroxynitrite and GSH-Px is first-order in each of the reactants, with an apparent second-order rate constant of 4.5 +/- 0.2 x 10(4) M-1 s-1 per monomer unit of enzyme.
S, Padmaja, G L, Squadrito, W A, Pryor
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The glutathione peroxidase activity of glutathione S-transferases

Biochimica et Biophysica Acta (BBA) - Enzymology, 1980
Glutatione transferases (RX:glutathione R-transferases, EC 2.5.1.18) B and AA were purified from rat liver to investigate the mechanism for their apparent GSH peroxidase activity (GSSG formation). Both transferases catalyze an overall reaction in which loss of cumene hydroperoxide is accompanied by a stoichiometric increase in GSSG.
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