title: 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.
authors.affiliation: Plant Research Laboratory, School of Life Sciences, Jawaharlal Nehru University, New Delhi, India.
authors.forename: R
authors.initials: R
authors.lastname: Deswal
authors.forename: S K
authors.initials: SK
authors.lastname: Sopory
mesh_terms: D001937:Brassica / Q000032:analysis*; D004586:Electrophoresis; D007700:Kinetics; D007791:Lactoylglutathione Lyase / Q000737:chemistry / Q000302:isolation & purification*; D008970:Molecular Weight; D010940:Plant Proteins / Q000737:chemistry / Q000302:isolation & purification; D013379:Substrate Specificity
chemical_list: D010940:Plant Proteins; D007791:Lactoylglutathione Lyase