Identification and characterization of a selenium-dependent glutathione peroxidase in Setaria cervi
| Autor: | Anchal Singh, Sushma Rathaur |
|---|---|
| Rok vydání: | 2005 |
| Předmět: |
Setaria Nematode
Biophysics Potassium cyanide chemistry.chemical_element Biochemistry Chromatography Affinity chemistry.chemical_compound Selenium Animals Molecular Biology chemistry.chemical_classification Glutathione Peroxidase biology Glutathione peroxidase Cell Biology Glutathione Chromatography Ion Exchange Molecular biology Enzyme assay Enzyme chemistry Setaria cervi biology.protein Electrophoresis Polyacrylamide Gel Female Peroxidase |
| Zdroj: | Biochemical and biophysical research communications. 331(4) |
| ISSN: | 0006-291X |
| Popis: | 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 approximately = 20 kDa. Selenium content of purified enzyme was estimated by atomic absorption spectroscopy and found to be 3.5 ng selenium/microg 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. |
| Databáze: | OpenAIRE |
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