This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Iizuka, M Articles by Kimura, A Search for Related Content PubMed PubMed Citation Articles by Iizuka, M Articles by Kimura, A

research-article

Purification and some properties of glutathione S-transferase from Escherichia coli B.

Research Institute for Food Science, Kyoto University, Japan.

ABSTRACT

Glutathione S-transferase was purified approximately 2,300-fold from cell extracts of Escherichia coli B with a 7.5% activity yield. The molecular weight of the enzyme was 45,000, and the enzyme appeared to consist of two homogeneous subunits. The enzyme was almost specific to 1-chloro-2,4-dinitrobenzene (Km, 1.43 mM) and glutathione (Km, 0.33 mM). The optimal pH and optimal temperature for activity were 7.0 and 50 degrees C, respectively, and the enzyme was stable from pH 5 to 11. The activity of the enzyme for 1-chloro-2,4-dinitrobenzene (3,2 mumol/min per mg of protein) was significantly lower than those of the enzymes from mammals, plants, and fungi.

This article has been cited by other articles:

• Tocheva, E. I., Fortin, P. D., Eltis, L. D., Murphy, M. E. P. (2006). Structures of Ternary Complexes of BphK, a Bacterial Glutathione S-Transferase That Reductively Dechlorinates Polychlorinated Biphenyl Metabolites. J. Biol. Chem. 281: 30933-30940 [Abstract] [Full Text]  
• Janowiak, B. E., Griffith, O. W. (2005). Glutathione Synthesis in Streptococcus agalactiae: ONE PROTEIN ACCOUNTS FOR {gamma}-GLUTAMYLCYSTEINE SYNTHETASE AND GLUTATHIONE SYNTHETASE ACTIVITIES. J. Biol. Chem. 280: 11829-11839 [Abstract] [Full Text]  
• Dhar, K., Dhar, A., Rosazza, J. P. N. (2003). Glutathione S-Transferase Isoenzymes from Streptomyces griseus. Appl. Environ. Microbiol. 69: 707-710 [Abstract] [Full Text]  
• Bartels, F., Backhaus, S., Moore, E. R. B., Timmis, K. N., Hofer, B. (1999). Occurrence and expression of glutathione-S-transferase-encoding bphK genes in Burkholderia sp. strain LB400 and other biphenyl-utilizing bacteria. Microbiology 145: 2821-2834 [Abstract] [Full Text]  
• Welihinda, A. A., Kaufman, R. J. (1996). The Unfolded Protein Response Pathway in Saccharomyces cerevisiae. OLIGOMERIZATION AND TRANS-PHOSPHORYLATION OF Ire1p (Ern1p) ARE REQUIRED FOR KINASE ACTIVATION. J. Biol. Chem. 271: 18181-18187 [Abstract] [Full Text]