MALDI mass sequencing and characterization of filarialglutathione-S-transferase |
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Authors: | Gupta Sarika Singh Anchal Yadav Marshleen Singh Kalyan Rathaur Sushma |
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Institution: | Molecular Biophysics Unit, Indian Institute of Sciences, Bangalore 560012, India. |
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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. |
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Keywords: | MALDI mass Glutathione-S-transferase Filariasis Setaria cervi |
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