Highly active dimeric and low-activity tetrameric forms of selenium-containing rat thioredoxin reductase 1

Free Radical Biology and Medicine

Volumn 46, Issue 7, 2009, Pages 893-904

  Rengby, Olle ^a   Cheng, Qing ^a   Vahter, Marie ^a   Jörnvall, Hans ^a   Arnér, Elias S J ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

Author keywords

Mass spectrometry; Oxidoreductase; Selenocysteine; Selenoprotein; Thioredoxin reductase; Turnover

Indexed keywords

ARSENOSOBENZENE; RECOMBINANT ENZYME; SELENIUM; SELENOCYSTEINE; THIOREDOXIN REDUCTASE 1;

ARTICLE; CROSS LINKING; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL;

ANIMALS; ARSENICALS; CLONING, MOLECULAR; CODON, TERMINATOR; CYSTEINE; ENZYME ACTIVATION; ESCHERICHIA COLI; MUTAGENESIS, SITE-DIRECTED; PROTEIN MULTIMERIZATION; RATS; RECOMBINANT PROTEINS; SELENIUM; SEPHAROSE; SUBSTRATE SPECIFICITY; THIOREDOXIN REDUCTASE 1;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; MAMMALIA; RATTUS;

EID: 61449217799     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2008.12.017     Document Type: Article

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