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Purification and properties of rat liver mitochondrial glutathione peroxidase.

Authors
  • Zakowski, J J
  • Tappel, A L
Type
Published Article
Journal
Biochimica et Biophysica Acta
Publisher
Elsevier
Publication Date
Sep 11, 1978
Volume
526
Issue
1
Pages
65–76
Identifiers
PMID: 28781
Source
Medline
License
Unknown

Abstract

Glutathione peroxidase (glutathione:hydrogen peroxide oxidoreductase, EC 1.11.1.9) 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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