A Piscine Glutathione S-Transferase Which Efficiently Conjugates the End-Products of Lipid Peroxidation

摘要

A cDNA clone for glutathione S-transferaseA (GSTA) form plaice (Pleur- onectes platessa) was expressed in Eschericia coli (E. coli) and purified to homogeneity by S-hexylglutathione affinity chromatography. When compared to literature values for a variety of purified mammalian GSTs, the heterologously expressed purified plaice enzyme had moderate activity towards the model sub- strate 1,2-chloro-2, 4-dinitrobenzene (CDNB) and exhibited a Km of 2.5±2mM and Vmax of 30.9±2.3μmol min~-1 mg~-1. it had little or no activity towards several other model GST substrates including 1,2-dinitrochloro-4-benzene (DCNB), ethacrynic acid (EA), and p-nitrobenzylchloride (NBC).