Abstract
Glutathione reductase (GR) expression and glutathione content were examined under oxidative stress conditions from the gram-positive clostridiale Enterococcus faecalis. The enzyme is found ubiquitously in gram-negative bacteria, and has been implicated in the defense against the oxidative burst response of the eukaryotic host immune system. We have purified to homogeneity the first GR from a gram-positive organism and demonstrated an increased expression of GR under hyperbaric oxygen conditions without a significant change in the total glutathione content. The kinetic parameters deduced for the E. faecalis GR are similar to those found for GR from yeast, E. col[, and human erythrocyte. The difference in the expression of the enzyme and substrate content suggest that the genes encoding the glutathione synthesizing enzymes are not linked to the oxygen-sensitive promoter of the glutathione reductase gene. Fur thermore, a critical examination of the kinetic parameters provides a plausible explanation for the distinction in the levels of expression of the substrate and.
Original language | English (US) |
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Pages (from-to) | A1319 |
Journal | FASEB Journal |
Volume | 11 |
Issue number | 9 |
State | Published - 1997 |
ASJC Scopus subject areas
- Biotechnology
- Biochemistry
- Molecular Biology
- Genetics