Human and murine cytosolic epoxide hydrolase: physical and structural properties

Int J Biochem. 1990;22(5):461-70. doi: 10.1016/0020-711x(90)90258-5.

Abstract

1. Human and murine liver cytosolic epoxide hydrolase (CEH) had an apparent Mw of 59,000 by SDS-PAGE. 2. Peptide maps of CNBr, trypsin and Staphylococcus 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. The CEHs shared antigenic determinants as determined by Western blotting. 4. Circular dichroism spectra indicate that human CEH had 39% alpha-helix. Uninduced and clofibrate induced murine CEH had 38 and 35% alpha-helix, respectively.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acids / analysis
  • Animals
  • Blotting, Western
  • Circular Dichroism
  • Clofibrate / pharmacology
  • Cyanogen Bromide
  • Cytosol / enzymology
  • Epoxide Hydrolases* / analysis
  • Epoxide Hydrolases* / biosynthesis
  • Epoxide Hydrolases* / metabolism
  • Humans
  • Isoelectric Point
  • Liver / enzymology*
  • Male
  • Mice
  • Mice, Inbred C57BL
  • Molecular Weight
  • Peptide Mapping
  • Protein Conformation
  • Serine Endopeptidases
  • Trypsin

Substances

  • Amino Acids
  • Epoxide Hydrolases
  • Serine Endopeptidases
  • glutamyl endopeptidase
  • Trypsin
  • Clofibrate
  • Cyanogen Bromide