Epoxide hydrolase activities in Drosophila melanogaster

L. G. Harshman, J. Casas, E. C. Dietze, B. D. Hammock

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27 Scopus citations


Epoxide hydrolase (EH) activity in Drosophila melanogaster cell fractions was characterized using juvenile hormone (JH III) and cis-stilbene oxide (CSO) as substrates. A comparison of detergents indicated that 0.3% Lubrol PX was relatively effective for solubilizing EH activity from the 20,000 and 100,000 g pellets. The effect of inhibitors, pH, temperature, salt and organic solvents on EH activity depended on the substrate and cell fraction tested, which suggested there were multiple activities present. For initial purification, polyethylene glycol was useful for precipitating EH activity from the 100,000 g supernatant.

Original languageEnglish (US)
Pages (from-to)887-894
Number of pages8
JournalInsect Biochemistry
Issue number8
StatePublished - 1991


  • Drosophila melanogaster
  • epoxide hydrolase
  • juvenile hormone


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