Human and murine cytosolic epoxide hydrolase: Physical and structural properties

Eric C. Dietze, Jacques Magdalou, Bruce D. Hammock

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

1. 1. Human and murine liver cytosolic epoxide hydrolase (CEH) had an apparent Mw of 59,000 by SDS-PAGE. 2. 2. Peptide maps of CNBr, trypsin and Slaphylococcus aureus V8 digests, as well as amino acid analysis, showed that human and murine CEH were similar. Uninduced and clofibrate induced murine CEH appeared qualitatively identical. 3. 3. The CEHs shared antigenic determinants as determined by Western blotting. 4. 4. Circular dichroism spectra indicate that human CEH had 39% α-helix. Uninduced and clofibrate induced murine CEH had 38 and 35% α-helix, respectively.

Original languageEnglish (US)
Pages (from-to)461-470
Number of pages10
JournalInternational Journal of Biochemistry
Volume22
Issue number5
DOIs
StatePublished - 1990

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Epoxide Hydrolases
Structural properties
Physical properties
Clofibrate
Circular Dichroism
Liver
Trypsin
Epitopes
Polyacrylamide Gel Electrophoresis
Western Blotting
Amino Acids
Peptides

ASJC Scopus subject areas

  • Biochemistry

Cite this

Human and murine cytosolic epoxide hydrolase : Physical and structural properties. / Dietze, Eric C.; Magdalou, Jacques; Hammock, Bruce D.

In: International Journal of Biochemistry, Vol. 22, No. 5, 1990, p. 461-470.

Research output: Contribution to journalArticle

Dietze, Eric C. ; Magdalou, Jacques ; Hammock, Bruce D. / Human and murine cytosolic epoxide hydrolase : Physical and structural properties. In: International Journal of Biochemistry. 1990 ; Vol. 22, No. 5. pp. 461-470.
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