Purification of an epoxide hydrolase from the midgut of the southern army worm (Spodoptera eridania)

C. A. Mullin, C. F. Wilkinson

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17 Scopus citations

Abstract

An epoxide hydrolase was solubilized with Cutscum® from microsomal fractions of southern army worm (Spodoptera eridania, Cramer) larval midguts. A 27-fold purification was achieved in high overall yield (38%) using ammonium sulphate fractionation, affinity chromatography (agarose with the ligand trans-9,10-epoxyoctadecanoic acid) and ion-exchange (DE-52) chromatography. The enzyme was judged highly pure by SDS-polyacrylamide gel electrophoresis and Ouchterlony double-diffusion analysis. The purified enzyme hydrolized styrene oxide and 1,2-epoxyoctane at the rates of 7.1 and 17.2 μmoles/mg protein/min respectively. Midgut epoxide hydrolase levels increased five-fold in specific activity and ninefold in total content during early development of the sixth larval instar and rapidly decreased at the onset of pupation. Hydrolase activity was enhanced two-fold following dietary exposure of the larvae to the mixed-function oxidase inducing agent pentamethylbenzene.

Original languageEnglish (US)
Pages (from-to)681-691
Number of pages11
JournalInsect Biochemistry
Volume10
Issue number6
DOIs
StatePublished - 1980

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