Purification and partial characterization of glyoxalase I from a higher plant Brassica juncea

Abstract
The glyoxalase I was purified from Brassica juncea by affinity chromatography on S-hexyl GSH sepharose 4B, Homogeneity of the protein was confirmed electrophoretically by a silver stained gel. Activity staining on a native starch gel also showed a single band. The effect of glutathione, methylglyoxal, and pH on enzyme kinetics was studied. Magnesium was found to stimulate the enzyme activity.