A comparative study on glyoxalase II from vertebrata.
S-2-hydroxyacylglutathione hydrolase (glyoxalase II) from the liver of animals belonging to the various vertebrate classes (Oryctolagus cuniculus, Gallus gallus, Python molurus, Rana esculenta, Esox lucius) have been purified from 100,000 g supernatants of liver homogenates, using acetone fractionation and affinity chromatography. Subsequent comparative studies were concerned with some molecular and kinetic properties. Isoelectric focusing gave evidence for a single form of liver glyoxalase II in O. cuniculus, P. molurus and E. lucius, while the enzyme from G. gallus and R. esculenta showed respectively two and three forms with different pI values. All studied enzymes are basic proteins. The relative molecular mass values range from 18,000 to 23,000. The various glyoxalases II do not display markedly different Kn or Ki values. Their stability behavior at different temperatures is also quite similar.
D000818:Animals; D002645:Chickens; D002846:Chromatography, Affinity; D007526:Isoelectric Point; D011817:Rabbits; D011893:Rana esculenta; D012487:Salmonidae; D012911:Snakes; D013045:Species Specificity; D013869:Thiolester Hydrolases / Q000302:isolation & purification*; D014714:Vertebrates / Q000378:metabolism*; D000099301:Hydroxyacylglutathione Hydrolase
D013869:Thiolester Hydrolases; D000099301:Hydroxyacylglutathione Hydrolase