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Journal of Nutrition Vol. 108 No. 6 June 1978, pp. 981-987
Copyright © 1978 by American Society for Nutrition
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Hepatic Cytosolic Non Selenium-Dependent Glutathione Peroxidase Activity: Its Nature and the Effect of Selenium Deficiency1

Richard A. Lawrence2, Linda K. Parkhill and Raymond F. Burk2

Liver Unit, Department of Internal Medicine and Department of Biochemistry, University of Texas Southwestern Medical School and Veterans Administration Hospital, Dallas, Texas 75235

Recent work has indicated the presence of a non selenium-dependent glutathione peroxidase activity in rat liver in addition to the selenium-dependent activity. The present study was undertaken to learn whether the glutathione S-transferases are responsible for the non selenium-dependent glutathione peroxidase activity and to study the effect of selenium deficiency on those enzymes. Glutathione S-transferase B was purified by an established method using carboxymethyl cellulose ion exchange chromatography and studied. It exhibited glutathione peroxidase activity toward cumene hydroperoxide and t-butyl hydroperoxide. A limiting Km of 0.55 mM was determined for cumene hydroperoxide. Sulfobromophthalein was found to be a competitive inhibitor with respect to cumene hydroperoxide of the glutathione peroxidase activity of glutathione S-transferase B. Selenium deficiency caused an increase in glutathione S-transferase activity. These results establish that glutathione S-transferase B contributes to the non selenium-dependent glutathione peroxidase activity in rat liver and show that it increases in selenium deficiency when the selenium-dependent glutathione peroxidase is decreased.

KEY WORDS: • selenium • glutathione peroxidase • glutathione S-transferase • liver • rat

1 Supported by NIH Grants R01 ES01017 and 5 T32 AM07100.

2 Present address: Department of Medicine, Louisiana State University Med. School, Shreveport, Louisiana 71130.

Manuscript received 14 November 1977.




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