Enterococcus faecalis glutathione reductase purification, characterization and expression under normal and hyperbaric o2 conditions

Mehul P. Patel, John S. Blanchard

Research output: Contribution to journalArticle

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 languageEnglish (US)
Pages (from-to)A1319
JournalFASEB Journal
Volume11
Issue number9
StatePublished - Dec 1 1997

ASJC Scopus subject areas

  • Biotechnology
  • Biochemistry
  • Molecular Biology
  • Genetics

Fingerprint Dive into the research topics of 'Enterococcus faecalis glutathione reductase purification, characterization and expression under normal and hyperbaric o2 conditions'. Together they form a unique fingerprint.

  • Cite this