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. 1990 Apr 9;263(1):77-9.
doi: 10.1016/0014-5793(90)80709-r.

Purification and study of a bacterial glutathione S-transferase

P Arca  1 , P García, C Hardisson, J E Suárez
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Free article

Purification and study of a bacterial glutathione S-transferase

P Arca et al. FEBS Lett. .
Free article

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 with Km values of 0.25 and 1.5 mM, respectively. Optima of pH and temperature were 7.5 and 35 degrees C. The activity was stimulated (30%) by ethylenediaminetetraacetic acid. The N-terminal amino acid sequence was: Met-Leu-Leu-Phe-Ile-Leu-Pro-Gly-Ala.

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