Purification and study of a bacterial glutathione S-transferase.
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Arca P, Garcia P, Hardisson C, Suarez JE
Purification and study of a bacterial glutathione S-transferase.
FEBS Lett. 1990 Apr 9;263(1):77-9.
- PubMed ID
- 2185038 [ View in PubMed]
- 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.