Identification and characterization of a selenium-dependent glutathione peroxidase in Setaria cervi

Journal Article · Fri Jun 17 04:00:00 EDT 2005 · Biochemical and Biophysical Research Communications

DOI:https://doi.org/10.1016/j.bbrc.2005.03.235· OSTI ID:20710801

Singh, Anchal ^[1]; Rathaur, Sushma ^[1]

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1. Department of Biochemistry, Faculty of Science, Banaras Hindu University, Varanasi 221005, UP (India)

Setaria cervi a bovine filarial parasite secretes selenium glutathione peroxidase during in vitro cultivation. A significant amount of enzyme activity was detected in the somatic extract of different developmental stages of the parasite. Among different stages, microfilariae showed a higher level of selenium glutathione peroxidase activity followed by males then females. However, when the activity was compared in excretory secretory products of these stages males showed higher activity than microfilariae and female worms. The enzyme was purified from female somatic extract using a combination of glutathione agarose and gel filtration chromatography, which migrated as a single band of molecular mass {approx}20 kDa. Selenium content of purified enzyme was estimated by atomic absorption spectroscopy and found to be 3.5 ng selenium/{mu}g of protein. Further, inhibition of enzyme activity by potassium cyanide suggested the presence of selenium at the active site of enzyme. This is the first report of identification of selenium glutathione peroxidase from any filarial parasite.

• OSTI ID: 20710801
• Journal Information: Biochemical and Biophysical Research Communications, Journal Name: Biochemical and Biophysical Research Communications Journal Issue: 4 Vol. 331; ISSN 0006-291X; ISSN BBRCA9
• Country of Publication: United States
• Language: English

Related Subjects

60 APPLIED LIFE SCIENCES
ABSORPTION SPECTROSCOPY
CATTLE
CHROMATOGRAPHY
CYANIDES
ENZYME ACTIVITY
GLUTATHIONE
IN VITRO
PARASITES
PEROXIDASES
POTASSIUM
SELENIUM