Heterologous expression of drug-metabolizing enzymes in cellular and whole animal models

A. P. Simula, M. B. Crichton, S. M. Black, S. Pemble, H. F.J. Bligh, J. D. Beggs, C. R. Wolf

Research output: Contribution to journalArticlepeer-review

10 Scopus citations


In this report we describe the heterologous expression of glutathione S-transferase (GST) and cytochrome P450 reductase (Red) in E. coli and Salmonella typhimurium. The same expression vectors could be applied to both systems and high levels of catalytically active GST and Red were obtained. Interestingly the level of expression was invariably higher in S. typhimurium. The level of the alpha class GST being up to 20% of the total bacterial protein. A further advantage of the salmonella system is that strains were used which can be applied to mutagenicity tests. This system was validated by demonstrating increasing mutation frequency of halogenated hydrocarbons in strains expressing the GST and increased cytotoxicity of mitomycin C in cells expressing P450 reductase.

Original languageEnglish (US)
Pages (from-to)3-20
Number of pages18
Issue number1-3
StatePublished - Oct 5 1993


  • Cytochrome P450
  • Glutathione transferases
  • Mutagenicity testing
  • P450 reductase
  • Salmonella typhimurium

ASJC Scopus subject areas

  • Toxicology


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