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Volumn 270, Issue 20, 1995, Pages 11761-11764
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Human thioredoxin reductase directly reduces lipid hydroperoxides by NADPH and selenocystine strongly stimulates the reaction via catalytically generated selenols
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Author keywords
[No Author keywords available]
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Indexed keywords
HYDROGEN PEROXIDE;
HYDROXYICOSATETRAENOIC ACID;
LIPID HYDROPEROXIDE;
SELENIUM DERIVATIVE;
SELENOCYSTINE;
THIOREDOXIN REDUCTASE;
ARACHIDONIC ACID METABOLISM;
ARTICLE;
DETOXIFICATION;
PRIORITY JOURNAL;
CATALYSIS;
CYSTINE;
GLUTATHIONE;
GLUTATHIONE TRANSFERASE;
HUMAN;
HYDROGEN PEROXIDE;
HYDROXYEICOSATETRAENOIC ACIDS;
LEUKOTRIENES;
LIPID PEROXIDATION;
LIPID PEROXIDES;
MODELS, BIOLOGICAL;
NADP;
ORGANOSELENIUM COMPOUNDS;
OXIDATION-REDUCTION;
PEROXIDES;
PLACENTA;
PROTEIN-SERINE-THREONINE KINASES;
PROTEIN-TYROSINE KINASE;
SELENOCYSTEINE;
SUPPORT, NON-U.S. GOV'T;
TERT-BUTYLHYDROPEROXIDE;
THIOREDOXIN;
THIOREDOXIN REDUCTASE (NADPH);
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EID: 0029031370
PISSN: 00219258
EISSN: None
Source Type: Journal
DOI: 10.1074/jbc.270.20.11761 Document Type: Article |
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Times cited : (275)
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References (0)
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