Purification and properties of rat liver mitochondrial glutathione peroxidase.
- Published Article
Biochimica et Biophysica Acta
- Publication Date
Sep 11, 1978
Glutathione peroxidase (glutathione:hydrogen peroxide oxidoreductase, EC 220.127.116.11) was purified from rat liver mitochondria. The enzyme was shown to be pure by polyacrylamide-gel electrophoresis and to contain multiple forms that differed in charge. Selenium was specifically associated with the enzyme. The enzyme was inhibited by iodoacetic acid and iodoacetamide in an unusual pattern of reduction by sulfhydryl compounds and pH dependency. The mitochondrial and cytoplasmic forms of the enzyme were compared, and an explanation of the inhibition patterns is offered.
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This record was last updated on 07/01/2016 and may not reflect the most current and accurate biomedical/scientific data available from NLM.
The corresponding record at NLM can be accessed at https://www.ncbi.nlm.nih.gov/pubmed/28781