Maldi Mass Sequencing and Characterization of Filarialglutathione-s-transferase.
From: Molecular Biophysics Unit, Indian Institute of Sciences, Bangalore 560012, India.
Biochemical and biophysical research communications
- Publish Date: May 2007
- ISSN: 0006-291X
- Volume: 356
- Issue: 2
- Pages: 381-5
- Medium: Print
- Language: English
- Citation (JAMA): Gupta Sarika, Singh Anchal, Yadav Marshleen, et al. Maldi Mass Sequencing and Characterization of Filarialglutathione-s-transferase.. Biochem. Biophys. Res. Commun. May 2007;356:381-5
Abstract
Glutathione-S-transferase has been detected in the somatic extract and excretory-secretory products of different life stages of Setaria cervi, a bovine filarial parasite. The enzyme was subjected to MALDI-TOF followed by mass spectrometry and the nearest match found was Pleuronectes platessa GST. Molecular mass of the purified enzyme was approximately 26 kDa as determined by SDS-PAGE and MALDI-TOF. Setaria cervi GST exhibited high activity towards 1-chloro-2,4-dinitrobenzene and ethacrynic acid. Kinetic analysis with respect to 1-chloro-2,4-dinitrobenzene and glutathione as substrate revealed a K(m) of 2.22 mM and 0.61 mM, respectively. The activity was inhibited significantly by Cibacron blue and alpha-tocopherol.
Mesh Headings (Keywords): Animals, Cattle, Glutathione Transferase, Helminth Proteins, Molecular Weight, Sequence Analysis, Protein, Setaria Nematode, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Check for Full Text / PubMed Unique Identifier (PMID): 17367761
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