NDLI: Purification and characterization of glutathione reductase (E.C. 1.8.1.7) from bovine filarial worms Setaria cervi.

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Purification and characterization of glutathione reductase (E.C. 1.8.1.7) from bovine filarial worms Setaria cervi.

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Purification and characterization of glutathione reductase (E.C. 1.8.1.7) from bovine filarial worms Setaria cervi.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Arora, Kavita Ahmad, Rumana Srivastava, Arvind K.
Description	Author Affiliation: Arora K ( K&S Partners, Intellectual Property Attorneys, 109, Sector 44, Gurgaon, 122 003 National Capital Region India ); Ahmad R ( Division of Biochemistry, Central Drug Research Institute, P.O. Box No. 173, Chattar Manzil Palace, Lucknow, 226 001 UP India.); Srivastava AK ( Division of Biochemistry, Central Drug Research Institute, P.O. Box No. 173, Chattar Manzil Palace, Lucknow, 226 001 UP India.)
Abstract	Antioxidant enzymes are the parasite's premier resource to defend themselves against reactive oxygen species generated by macrophages, neutrophils and eosinophils of the host. These enzymes may be particularly important for parasites involved in chronic infections, such as parasitic helminths. Glutathione (GSH) and glutathione reductase (GR) are parts of the GSH redox cycle, which protects cells against damage by oxidants. Both GSH and GR are present in significant amounts in Setaria cervi female worms. GR has a central role in glutathione metabolism and as such is a potential target for chemotherapy. The aim of the work was to purify and characterize GR from S. cervi and to compare the properties of the helminth enzyme with its mammalian counterpart. GR was purified from filarial parasites S. cervi and preliminary steady state kinetics was performed. The purified protein was observed to be a dimer of 55 kDa subunit as evident from SDS-PAGE analysis. Kinetic studies revealed significant differences in the properties of S. cervi GR from its mammalian counterpart which may be exploited in chemotherapy of filariasis. Filarial GR is thus proposed as a potential drug target.
File Format	HTM / HTML
ISSN	09717196
e-ISSN	09750703
DOI	10.1007/s12639-012-0138-8
Journal	Journal of Parasitic Diseases
Issue Number	1
Volume Number	37
Language	English
Publisher	Springer
Publisher Date	2013-04-01
Publisher Place	India
Access Restriction	Open
Subject Keyword	Discipline Parsitology
Content Type	Text
Resource Type	Article
Subject	Parasitology

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Purification and characterization of glutathione reductase (E.C. 1.8.1.7) from bovine filarial worms Setaria cervi

Morphological characterization of Setaria worms collected from cattle.

Identification and characterization of novel membrane-bound PRL protein tyrosine phosphatases from Setaria cervi, a bovine filarial parasite

Morphological characterization of Setaria worms collected from cattle

Kinetic Characterisation of Phosphofructokinase Purified from Setaria cervi: A Bovine Filarial Parasite

Identification of GR and TrxR systems in Setaria cervi: Purification and characterization of glutathione reductase.

Modulation of phosphofructokinase (PFK) from Setaria cervi, a bovine filarial parasite, by different effectors and its interaction with some antifilarials

Modulation of phosphofructokinase (PFK) from Setaria cervi, a bovine filarial parasite, by different effectors and its interaction with some antifilarials

Tissue localization of collagenase and leucine aminopeptidase in the bovine filarial parasite Setaria cervi

Purification and characterization of glutathione reductase (E.C. 1.8.1.7) from bovine filarial worms Setaria cervi.

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Purification and characterization of glutathione reductase (E.C. 1.8.1.7) from bovine filarial worms Setaria cervi

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