Optimization of assay conditions for epoxide metabolizing enzymes in Trichoplusia ni

James A. Ottea, Bruce D. Hammock

Research output: Contribution to journalArticlepeer-review

9 Scopus citations


The optimization of assay conditions for glutathione S-transferase and epoxide hydrolase activities in the cabbage looper (Trichoplusia ni [Hübner], Lepidoptera; Noctuidae) using trans and cis-stilbene oxides as substrates are reported. Glutathione S-transferase activity was predominantly cytosolic, and it was much greater in the fat body than the midgut. Differences in pH optima and rates of conjugation were seen between the trans and cis isomers of the substrate. In contrast, epoxide hydrolase activity was predominantly microsomal and was highest in the midgut. Patterns of substrate selectivity and pH optima differed between these two tissues. These data reflect the complexity of insect epoxide metabolism and suggest the involvement of multiple forms of these enzymes.

Original languageEnglish (US)
Pages (from-to)319-325
Number of pages7
JournalInsect Biochemistry
Issue number2
StatePublished - 1986


  • cis-stilbene oxide
  • epoxide
  • epoxide hydrolase
  • glutathione S-transferase
  • Insect
  • Lepidoptera
  • Noctuidae
  • trans-stilbene oxide
  • Trichoplusia ni (Hübner)


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