Analysis of glyoxalase-I from normal and tumor tissue from human colon

Biochim Biophys Acta. 1993 Oct 20;1182(3):311-6. doi: 10.1016/0925-4439(93)90074-b.


Glyoxalase-I (Gly-I) is part of the glyoxalase system which converts methylglyoxal to D-lactic acid via an S-D-lactoylglutathione intermediate. This glutathione (GSH)-binding protein was purified from human colon tumors and corresponding normal tissue. The GSH-affinity purified fraction from normal human colon tissue showed enzyme activity of 30.6 +/- 11.5 mumol/min per mg protein, with methylglyoxal as substrate. Corresponding fractions from carcinomas showed significantly elevated Gly-I activity of 54.5 +/- 15 mumol/min per mg protein. Polyclonal antibodies made against human Gly-I cross-reacted weakly with mouse liver Gly-I but not with yeast Gly-I. Isoelectric points of Gly-I from human, mouse and yeast were determined to be 4.6, 4.9 and 7.0, respectively, by horizontal IEF. Immunohistochemical analysis confirmed the increase of Gly-I in human colon carcinoma in 16 out of 21 samples when compared to corresponding normal tissue. The elevated levels of Gly-I in colon tumors may be an indicator of the enhanced proliferative status of the neoplastic condition.

Publication types

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

MeSH terms

  • Animals
  • Antibodies / immunology
  • Biomarkers, Tumor / analysis
  • Colonic Neoplasms / enzymology*
  • Colonic Neoplasms / pathology
  • Humans
  • Immunohistochemistry
  • Isoelectric Focusing
  • Lactoylglutathione Lyase / analysis*
  • Lactoylglutathione Lyase / immunology
  • Lactoylglutathione Lyase / isolation & purification
  • Mice
  • Saccharomyces cerevisiae


  • Antibodies
  • Biomarkers, Tumor
  • Lactoylglutathione Lyase