Evidence for the occurrence of selenium-independent glutathione peroxidase activity in rat liver microsomes

Rat liver microsomes exhibit selenium-independent glutathione peroxidase activity which is associated with glutathione S-transferase activity. The peroxidase activity is not due to contamination with either soluble selenium-dependent or selenium-independent glutathione peroxidase activities of the c...

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Veröffentlicht in:Biochemical and biophysical research communications 1981-08, Vol.101 (3), p.970-978
Hauptverfasser: Channa Reddy, C., Tu, Chen-Pei D., Burgess, John R., Ho, Chih-Ying, Scholz, Richard W., Massaro, Edward J.
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Sprache:eng
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Zusammenfassung:Rat liver microsomes exhibit selenium-independent glutathione peroxidase activity which is associated with glutathione S-transferase activity. The peroxidase activity is not due to contamination with either soluble selenium-dependent or selenium-independent glutathione peroxidase activities of the cytosol. N-Ethylmaleimide treatment which stimulates rat liver microsomal glutathione transferase activity concomitantly stimulates the glutathione peroxidase activity. In contrast, N-ethylmaleimide depresses both enzyme activities of the cytosol. A protein exhibiting both glutathione peroxidase and glutathione transferase activity was isolated from the microsomes and purified to homogeneity by DEAE cellulose ion-exchange and S-hexylglutathione Sepharose 6B affinity chromatography.
ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(81)91844-1