Rapid purification of glutarthione S-transferase from Neodiplostomum seoulense |
Min-Ho Choi, Young-Bae Chung |
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Abstract |
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 column
chromatography. The purification fold and recovery rate were 9.7 and 50.4%, respectively. The molecular weight of the
purified GST was estimated to be 28 kDa on 7.5-15% gradient SDS-PAGE. From this study, the authors firstly reported the
presence of GST from N. seoulense and further studies such as inhibition test, subclass of GST as well as immunological
studies would be required. |
Key Words:
glutathione S-transferase, Neodiplostomum seoulense, intestinal trematode |
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