Glutathione peroxidase activity in selenium-deficient rat liver

Glutathione peroxidase activity in the liver supernatant from rats fed a Se-deficient diet for 2 weeks was 8% of control when measured with H 2O 2 but 42% of control when assayed with cumene hydroperoxide. Two peaks of glutathione peroxidase activity were present in the Sephadex G-150 gel filtration...

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Bibliographic Details
Published inBiochemical and biophysical research communications Vol. 71; no. 4; pp. 952 - 958
Main Authors Lawrence, Richard A., Burk, Raymond F.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 23.08.1976
Subjects
Animals
Drug Stability
Female
Glutathione Peroxidase - isolation & purification
Glutathione Peroxidase - metabolism
Hot Temperature
Liver - drug effects
Liver - enzymology
Molecular Weight
Peroxidases - metabolism
Rats
Selenium - deficiency
Selenium - pharmacology
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Summary:Glutathione peroxidase activity in the liver supernatant from rats fed a Se-deficient diet for 2 weeks was 8% of control when measured with H 2O 2 but 42% of control when assayed with cumene hydroperoxide. Two peaks of glutathione peroxidase activity were present in the Sephadex G-150 gel filtration chromatogram of rat liver supernatant when 1.5 mM cumene hydroperoxide was used as substrate. Only the first peak was detected when 0.25 mM H 2O 2 was used as substrate. The first peak was absent from chromatograms of Se-deficient rat liver supernatants; but the second peak, which eluted at a position corresponding to M.W. = 39,000, appeared unchanged. The second peak thus represents a second glutathione peroxidase activity which catalyzes the destruction of organic hydroperoxides but has little activity toward H 2O 2 and which persists in severe selenium deficiency.
Bibliography:ObjectType-Article-1
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ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(76)90747-6