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RESEARCH PRODUCT
Elevation of hepatic epoxide hydratase activity by ethoxyquin is due to increased synthesis of the enzyme.
Regine Kahlsubject
MaleAntioxidantmedicine.medical_treatmentBiophysicsCycloheximideBiochemistrySubstrate Specificitychemistry.chemical_compoundEthoxyquinmedicineAnimalsEnzyme inducerBenzopyrenesCycloheximideMolecular Biologychemistry.chemical_classificationEpoxide HydrolasesEthoxyquinbiologyLiver cellCell BiologyRatsEnzymechemistryBiochemistryEnzyme Inductionbiology.proteinMicrosomeMicrosomes LiverQuinolinesLeucinedescription
Abstract Feeding of the antioxidant ethoxyquin to rats leads to an increase of epoxide hydratase activity in liver microsomes. The apparent half life of the increase is 3–4 days. Elevation of epoxide hydratase activity is also obtained by intraperitoneal treatment of mice with ethoxyquin. This elevation is prevented by concomitant treatment with cycloheximide. When radiolabelled leucine is incorporated into microsomal protein by liver cell fractions from either ethoxyquin-fed or untreated rats, gel electrophoresis reveals that ethoxyquin feeding increases incorporation into epoxide hydratase. These results suggest that the elevation of epoxide hydratase activity by ethoxyquin is due to increased biosynthesis of the enzyme, i.e. enzyme induction.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1980-07-01 | Biochemical and biophysical research communications |