Results 291 to 300 of about 508,182 (337)
Some of the next articles are maybe not open access.

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
L, Flohé, I, Brand
openaire   +2 more sources

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   +2 more
openaire   +2 more sources

Plant glutathione peroxidases

Physiologia Plantarum, 1997
Oxidative stress in plants causes the induction of several enzymes, including superoxide dismutase (EC 1.15.1.1), ascorbate peroxidase (EC 1.11.1.11) and glutathione reductase (EC 1.6.4.2). The first two are responsible for converting superoxide to H2O2 and its subsequent reduction to H2O, and the third is involved in recycling of ascorbate ...
Yuval Eshdat   +3 more
openaire   +1 more source

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
openaire   +2 more sources

Glutathione Peroxidase-4

2011
Within the family of glutathione peroxidases (GPxs), GPx-4 is the sole monomeric enzyme that contains Sec at the active site. Phylogenetically, it is closer to the Cys-containing homologues (CysGPx) of invertebrata and vertebrata than to the tetrameric GPxs of vertebrata containing Sec.
MAIORINO, MATILDE   +5 more
openaire   +2 more sources

The glutathione peroxidase family: Discoveries and mechanism.

Free Radical Biology & Medicine, 2022
L. Flohé, S. Toppo, L. Orian
semanticscholar   +1 more source

Phylogenetic distribution of glutathione peroxidase

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1979
1. The enzyme glutathione peroxidase (E.C.1.11.1.9), known to be a selenoprotein from mammalian sources, was detected in the following vertebrates: fish, frog, salamander, and turtle. 2. Among invertebrates, the enzyme was detected in crayfish and snail but not in insects or earthworm. 3.
J, Smith, A, Shrift
openaire   +2 more sources

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   +2 more
openaire   +2 more sources

Electrophoretic polymorphism of glutathione peroxidase

Annals of Human Genetics, 1974
SUMMARYA method for the detection of glutathione peroxidase after electrophoresis on starch gel has been devised. Blood samples from 780 persons of Caucasian or Negro origin were studied. An electrophoretically fast enzyme, designated as the Thomas variant, was found in 6·4 % of 392 Negro donors and 0·8 % of 388 Caucasian donors.
E, Beutler, C, West, B, Beutler
openaire   +2 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.
H E, Ganther, R J, Kraus
openaire   +2 more sources

Home - About - Disclaimer - Privacy