MALDI mass sequencing and characterization of filarialglutathione-S-transferase.
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.
Gupta
Sarika
S
Molecular Biophysics Unit, Indian Institute of Sciences, Bangalore 560012, India.
Singh
Anchal
A
Yadav
Marshleen
M
Singh
Kalyan
K
Rathaur
Sushma
S
D000818:Animals; D002417:Cattle; D005982:Glutathione Transferase / Q000737:chemistry / Q000378:metabolism*; D015801:Helminth Proteins / Q000737:chemistry / Q000378:metabolism*; D008970:Molecular Weight; D020539:Sequence Analysis, Protein; D017182:Setaria Nematode / Q000201:enzymology*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D015801:Helminth Proteins; D005982:Glutathione Transferase