Biochemical characterization of a variant form of cytosolic epoxide hydrolase induced by parental exposure to N-ethyl-N-nitrosourea

Jaffar Nourooz-Zadeh, Bruce S. Winder, Eric C. Dietze, Carol S. Giometti, Sandra L. Tollaksen, Bruce D. Hammock

Research output: Contribution to journalArticle

5 Scopus citations

Abstract

1. ENU4 mice express a protein variant originally detected in a CBF1 mouse sired by a C57BL/6 mouse exposed to N-ethyl-N-nitrosourea. It appears to be an isolelectric point variant of cytosolic epoxide hydrolase. Affinity purified cytosolic epoxide hydrolase from ENU4 mice has a pI of approximately 5.1 compared to 5.6 in other mouse strains. 2. Clofibrate induced cytosolic epoxide hydrolase to similar levels in five strains of mice. However, CBF1 and ENU4 mice were more sensitive to the induction of palmitoyl CoA oxidase activity. 3. Except for isoelectric point, the physico- and immunochemical properties of cytosolic epoxide hydrolase from ENU4 mice were similar to those of the other mouse strains. Substrate specificities for five of six substrates tested were also similar.

Original languageEnglish (US)
Pages (from-to)207-214
Number of pages8
JournalComparative Biochemistry and Physiology. Part C, Comparative
Volume103
Issue number1
DOIs
StatePublished - 1992

ASJC Scopus subject areas

  • Pharmacology
  • Immunology

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