Advertisement

Isolation and Immobilization of Porcine Ligandin with Glutathione Transferase Activity

  • Lafranco Callegaro
  • Angelo Fontana

Abstract

The glutathione transferases (EC 2.5.1.18) are basic proteins of about 45, 000 daltons composed of two subunits (-3). They appear to play a fundamental role in the detoxification of noxious materials; they catalyze the conjugation of glutathione to potential alkylating agents of hydrophobic nature. The glutathione conjugates are further metabolized to mercapturic acids which are then excreted. Indeed, the glutathione transferases possess also binding properties for a large number of lipophilic compounds, including bilirubin, penicillin, bromosulfophtalein, azodye carcinogens, steroids, metabolites, drugs and various organic anions (1,4,5). Thus, these enzymes, under the generic term of ligandin, appear to act in the liver as binding proteins in a manner analogous to albumin, which serves this function in serum. The biological importance of these enzymes is reflected by the fact that man normally has about 10 percent of its extractable protein from liver as glutathione transferases (6). This report is concerned with the isolation and immobilization of ligandin from porcine liver.

Keywords

Immobilize Enzyme Organic Anion Lipophilic Compound Soluble Enzyme Glutathione Transferase 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    LITWAK, G., KETTERER, B. & ARIAS, I.M. Nature 234; 466, 1971.CrossRefGoogle Scholar
  2. 2.
    HABIG, W.H., PABST, M.J., & JAKOBY, W. J. J. Biol. Chem. 249: 7130, 1974.Google Scholar
  3. 3.
    JAKOBY, W.B. Adv. Enzymol. 46: 383, 1978.Google Scholar
  4. 4.
    HABIG, W.H., pabst, M.J., fleishner, G., gatmaitan, Z., ARIAS, I.M., & JAKOBY, W.B. Proc. Natl. Acad. Sei. USA 71: 3879, 1974.CrossRefGoogle Scholar
  5. 5.
    KAMISAKA, K., HABIG, W.H., KETLEY, J.N., ARIAS, I.M., & JAKOBY, W.B. Eur. J. Biochem. 60: 153, 1975.CrossRefGoogle Scholar
  6. 6.
    JAKOBY, W.B., KETLEY, J.N., & HABIG, W.H. in Glutathione: Metabolism and Function (I. M. Arias and W. B. Jakoby, eds.), Raven Press, New York, NY, 1976, pp. 213–223.Google Scholar
  7. 7.
    GRAHNEN, A. & SJOHOLM, I. Eur. J. Biochem. 80: 573, 1977.CrossRefGoogle Scholar
  8. 8.
    WHELAN, G., HOCH, J. & COMBES, B. J. Lab. Chim. Med. 75: 542, 1970.Google Scholar
  9. 9.
    CUATRECASAS, P. J. Biol. Chem. 245: 3059, 1970.Google Scholar

Copyright information

© Plenum Press, New York 1980

Authors and Affiliations

  • Lafranco Callegaro
    • 1
  • Angelo Fontana
    • 2
  1. 1.Laboratory of EnzymologySorin BiomedicaSaluggiaItaly
  2. 2.Institute of Organic Chemistry, Biopolymer Research Center, C.N.R.University of PadovaPadovaItaly

Personalised recommendations