| Literature DB >> 2185038 |
P Arca1, P García, C Hardisson, J E Suárez.
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.Entities:
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Year: 1990 PMID： 2185038 DOI： 10.1016/0014-5793(90)80709-r
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124