The purification and characterization of liver glyoxalase I from normal mice and from mice bearing a lymphosarcoma.

Glyoxalase I has been purified from the livers of normal DBA/1J mice (565-fold) and mice bearing a lymphosarcoma (348-fold). There was a significant difference in the fractionation patterns of the glyoxalase I activities from the two sources. Molecular weight determinations for which Sephadex gel filtration was used were conducted on the purified enzymes. The estimated molecular weights are 48,000 for the normal liver enzyme and 60,000 for the "tumor liver" enzyme. Treatment with guanidine-HCl has no effect on the molecular weight of liver glyoxalase I from normal mice; however, similar treatment of the liver enzyme from tumor-bearing mice decreases the molecular weight of catalytically active enzyme to approximately 23,000. The Km values of the enzymes are similar. Studies with the tumor (lymphosarcoma) enzyme indicate that the liver enzyme from tumor-bearing mice is not of tumor origin. The results of the investigation suggest that the glyoxalase 1 enzyme in the liver of mice bearing a lymphosarcoma is modified due to the presence of the tumor.