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. 1989;94(2):323-7.
doi: 10.1016/0305-0491(89)90350-7.

Selenium-independent glutathione peroxidase activity associated with glutathione S-transferase from the housefly, Musca domestica

T W Simmons  1 , I S Jamall, R A Lockshin
Affiliations

Selenium-independent glutathione peroxidase activity associated with glutathione S-transferase from the housefly, Musca domestica

T W Simmons et al. Comp Biochem Physiol B. 1989.

Abstract

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.

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