Two cytosolic glutathione S-transferase (GST) classes were isolated and characterized from California halibut (Paralichthys californicus) liver. Nanospray liquid chromatography-tandem mass spectrometry (LC-MS/MS) was used to elucidate peptide sequences and the proteins were identified as theta and alpha by searching against the NCBI non-redundant database (nrDB). Catalytic activity of the cytosolic GSTs towards 1-chloro-2,4-dinitrobenzene (CDNB) was determined to be 0.23+/-0.003 U/mg cytosolic protein.
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