Rapid purification of glutarthione S-transferase from Neodiplostomum seoulense

The authors partially purified glutathione S-transferase (GST) of Neodiplostomum seoulense monitoring its activity using 1-chloro-2,4-dinitrobenzene (CDNB). The enzyme was partially purified using glutathione?agarose affinity columnchromatography. The purification fold and recovery rate were 9.7 and 50.4%, respectively. The molecular weight of thepurified GST was estimated to be 28 kDa on 7.5-15% gradient SDS-PAGE. From this study, the authors firstly reported thepresence of GST from N. seoulense and further studies such as inhibition test, subclass of GST as well as immunologicalstudies would be required.