Abstract
Multiple glutathione S-transferase (GST) isoenzymes from Galleria mellonella have been purified by use of a combination of BSP affinity chromatography and isoelectric focusing to give catalytically active proteins isoelectric at pI 5.2, 6.9, 7.7 and 8.2. All isoforms were active with 1-chloro-2,4-dinitrobenzene (CDNB), 3-4-dichloro-nitrobenzene (DCNB) and were capable of cleaving β-methyl-umbelliferyl acetate (MUA). The pI 8.2 isoenzyme had by far the greatest activity with respect to CDNB. All four isoforms had activities of approximately the same magnitude with the other two substrates. All isoforms had detectable activity with monobromobimane and this substrate, or β-methyl umbelliferyl acetate could be used to localize the isoenzymes in electrophoresis gels by virtue of the fluorescent products of the reactions.
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