title: MALDI mass sequencing and characterization of filarialglutathione-S-transferase.
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.
authors: Molecular Biophysics Unit, Indian Institute of Sciences, Bangalore 560012, India.
authors: Sarika
authors: S
authors: Gupta
authors: Anchal
authors: A
authors: Singh
authors: Marshleen
authors: M
authors: Yadav
authors: Kalyan
authors: K
authors: Singh
authors: Sushma
authors: S
authors: Rathaur
mesh_terms: 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
chemical_list: D015801:Helminth Proteins; D005982:Glutathione Transferase