Purification and study of a bacterial glutathione S‐transferase

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Abstract
A glutathione S-transferase from Escherichia coli has been purified approximately 800-fold with an 11% activity yield by passage through DEAE Sephacel and glutathione-agarose affinity columns. Its functional form is a homodimer of two 24 000 Da polypeptides that catalyzes the binding of glutathione and 1-chloro-2,4-dinitrobenzene withK m values of 0.25 and 1.5 mM, respectively. Optima of pH and temperature were 7.5 and 35°C. The activity was stimulated (30%) by ethylenediaminetetraacetic add. The N-tenninal amino acid sequence was: Met-Leu-Leu-Phe-Ile-Leu-Pro-Gly-Ala.