PMID:2185038
| Citation |
Arca, P, García, P, Hardisson, C and Suárez, JE (1990) Purification and study of a bacterial glutathione S-transferase. FEBS Lett. 263:77-9 |
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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 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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| Keywords |
Amino Acid Sequence; Chromatography, Affinity; Chromatography, Ion Exchange; Electrophoresis, Polyacrylamide Gel; Escherichia coli/enzymology; Glutathione Transferase/isolation & purification; Glutathione Transferase/metabolism; Kinetics; Macromolecular Substances; Molecular Sequence Data; Molecular Weight |
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