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Two anionic isoenzymes of glutathione S-transferase (EC 2.5.1.18 ), GST θ and GST μ, have been purified from the eyes of the shrimp Penaseus japonicus by using a combination of S- hexyl- glutathione affinity column chromatography and Mono Q fast protein liquid chromatography (f.p.l.c.). The purified GST θ was a dimeric enzyme protein with subunit Mr abount 25 kDa. HPLC reverse phase C4 column analysis of various shrimp tissues indicated that the ratio of GST θ vs. GST μ was highest in the eye and gill. HPLC reverse phase C4 column analysis demostrated that corticosterone was selective binding to GST θ. Glutathione influenced the binding of corticosterone to the GST θ.
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