Selenium-independent glutathione peroxidase activity associated with glutathione S-transferase from the housefly, Musca domestica.
1. A glutathione S-transferase having Se-independent glutathione peroxidase activity was isolated from 100,000 g supernatant from housefly homogenate. 2. The specific activity of the partially purified Se-independent glutathione peroxidase was 1776 nmol NADPH oxidized/min/mg protein, representing an 87-fold purification. 3. The Mr of this enzyme was estimated to be 37,000 and 26,000 by gel filtration chromatography and gel electrophoresis, respectively. 4. Selenium-dependent glutathione peroxidase activity could not be detected in this same supernatant. 5. Se-independent glutathione peroxidase activity should be considered in future studies of the insect antioxidant defense system.
Simmons
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TW
Department of Biological Sciences, St. John's University, Jamaica, NY 11439.
Jamall
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IS
Lockshin
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RA
D000818:Animals; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D005979:Glutathione Peroxidase / Q000302:isolation & purification / Q000378:metabolism*; D005982:Glutathione Transferase / Q000302:isolation & purification / Q000378:metabolism*; D006793:Houseflies / Q000201:enzymology*; D008970:Molecular Weight; D009249:NADP / Q000378:metabolism; D010084:Oxidation-Reduction; D012643:Selenium / Q000494:pharmacology
D009249:NADP; D005979:Glutathione Peroxidase; D005982:Glutathione Transferase; D012643:Selenium