Purification and characterization of two human liver carboxylesterases

https://doi.org/10.1016/0020-711X(89)90149-3Get rights and content

Abstract

  • 1.

    1. Two carboxylesterases (EC 3.1.1.1) purified from human livers were distinguished by pi (isoelectric point), nondenaturing polyacrylamide gel electrophoresis, molecular weight, catalytic activity, N-tenninus and immunological cross-reactivity.

  • 2.

    2. The low pI carboxylesterase has not been reported previously.

  • 3.

    3. Numerous bands seen when each enzyme was focused on analytical IEF gels could not be separated.

  • 4.

    4. When sections of the band pattern was refocused, the original complete band pattern was generated.

  • 5.

    5. Both the mid and low pI carboxylesterases had catalytic activity for xenobiotics as well as medium and long chain fatty acid esters.

References (29)

  • R. Mentlein et al.

    Genetic identification of rat liver carboxylesterases isolated in different laboratories

    Biochim. biophys. Acta

    (1987)
  • R.E. Talcott

    Hepatic and extrahepatic malathion carboxylesterases. Assay and localization in the rat

    Toxic. Appl. Pharmac.

    (1979)
  • G.P. Albaugh et al.

    Transfer of proteins from plastic-backed isoelectric focusing gels to nitrocellulose paper

    Electrophoresis

    (1987)
  • N.A. Atanasov

    Purification and molecular weight of human liver carboxylesterase (EC 3.1.1.1)

    Rev. Roum. Biochim.

    (1976)
  • Cited by (33)

    • Regulation of Xenobiotic Metabolism in the Liver

      2010, Comprehensive Toxicology, Second Edition
    • Structural organization and characterization of the promoter region of a human carboxylesterase gene

      1997, Biochimica et Biophysica Acta - Gene Structure and Expression
    View all citing articles on Scopus
    View full text