Human Thioredoxin Reductase Directly Reduces Lipid Hydroperoxides by NADPH and Selenocystine Strongly Stimulates the Reaction via Catalytically Generated Selenols
Open Access
- 1 May 1995
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 270 (20), 11761-11764
- https://doi.org/10.1074/jbc.270.20.11761
Abstract
No abstract availableKeywords
This publication has 30 references indexed in Scilit:
- Mutagenesis of structural half-cystine residues in human thioredoxin and effects on the regulation of activity by selenodiglutathioneBiochemistry, 1993
- Mammalian lipoxygenases: molecular structures and functionsBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1992
- Reactive oxygen-reducing and protein-refolding activities of adult t cell leukemia-derived factor /human thioredoxinBiochemical and Biophysical Research Communications, 1992
- Selenocysteine: the 21st amino acidMolecular Microbiology, 1991
- Oxygen radical chemistry of polyunsaturated fatty acidsFree Radical Biology & Medicine, 1989
- Rearrangement of 15-hydroperoxy-eicosatetraenoic acid (15-HPETE) during incubations with hemoglobin: A model for platelet lipoxygenase metabolismProgress in Lipid Research, 1981
- The level and half‐life of glutathione in human plasmaFEBS Letters, 1980
- Glutathione peroxidase activity of D,L-selenocystine and selenocystamineBiochemical and Biophysical Research Communications, 1980
- Reduction of RibonucleotidesAnnual Review of Biochemistry, 1979
- Selenium: Biochemical Role as a Component of Glutathione PeroxidaseScience, 1973