Novel glutathione conjugates formed from epoxyeicosatrienoic acids (EETs)

Marshall E. Spearman, Russell A. Prough, Ronald W. Estabrook, J R Falck, Sukumar Manna, Kenneth C. Leibman, Robert C. Murphy, Jorge Capdevila

Research output: Contribution to journalArticlepeer-review

69 Scopus citations


The catalysis of glutathione (GSH) conjugation to epoxyeicosatrienoic acids (EETs) by various purified isozymes of glutathione S-transferase was studied. A GSH conjugate of 14,15-EET was isolated by HPLC and TLC; this metabolite contained one molecule of EET and one molecule of GSH. Fast atom bombardment mass spectrometry of the isolated metabolite confirmed the structure as a GSH conjugate of 14,15-EET. Studies designed to determine the isozyme specificity of this reaction demonstrated that two isozymes, 3-3, and 5-5, efficiently catalyzed this conjugation reaction. The Km values for 14,15-EET were approximately 10 μm and the Vmax values ranged from 25 to 60 nmol conjugate formed min-1 mg-1 purified transferase 3-3 and 5-5. The 5,6-, 8,9-, and 11,12-EETs were also substrates for the reaction, albeit at lower rates. These results demonstrate that the EETs can serve as substrates for the cytosolic glutathione S-transferases.

Original languageEnglish (US)
Pages (from-to)225-230
Number of pages6
JournalArchives of Biochemistry and Biophysics
Issue number1
StatePublished - Oct 1985

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology


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