A two-step purification of mouse liver glyoxalase I and evidence of its dimeric constitution.
Glyoxalase I (S-lactoyl-glutathione methylglyoxal-lyase (isomerizing), EC 4.4.1.5) was purified from Swiss mouse liver to homogeneity by a rapid, two-step procedure involving hydrophobic and affinity chromatography. Homogeneity was established by multiple electrophoretic determinations and by sedimentation equilibrium centrifugation. The purified enzyme exhibited a specific activity of 944 I.U./mg protein an has a molecular weight of 43 000. The enzyme was shown to be a dimer by sodium dodecyl sulfate disc gel electrophoresis and is apparently composed of identical subunits of molecular weights approximating 21 500.
D000818:Animals; D002846:Chromatography, Affinity; D007791:Lactoylglutathione Lyase / Q000302:isolation & purification*; D008099:Liver / Q000201:enzymology*; D008190:Lyases / Q000302:isolation & purification*; D046911:Macromolecular Substances; D008722:Methods; D051379:Mice; D008970:Molecular Weight
D046911:Macromolecular Substances; D008190:Lyases; D007791:Lactoylglutathione Lyase