Characterization of Enterobacter cloacae and E. sakazakii by electrophoretic polymorphism of acid phosphatase, esterases, and glutamate, lactate and malate dehydrogenases.
Acid phosphatase, esterases, and glutamate, lactate and malate dehydrogenases of 34 strains of Enterobacter cloacae and 22 strains of Enterobacter sakazakii were analysed by horizontal polyacrylamide agarose gel electrophoresis and by isoelectrofocusing in thin-layer polyacrylamide gel. The two species could be separated on the basis of distinct electrophoretic patterns of all enzymes analysed. Glutamate dehydrogenase and acid phosphatase were detected exclusively in E. cloacae, whereas esterase bands were more intensively stained in E. sakazakii. For each species, two zymotypes could be distinguished, on the basis of electrophoretic mobilities of malate dehydrogenase and banding patterns of esterase for E. cloacae, and by both isoelectric point and electrophoretic mobilities of an esterase and of lactate and malate dehydrogenases for E. sakazakii. The high degree of enzyme polymorphism within the two species permitted precise identification of strains. The variations in electrophoretic patterns might therefore provide useful epidemiological markers.
D000135:Acid Phosphatase / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D004754:Enterobacter / Q000201:enzymology*; D004755:Enterobacteriaceae / Q000201:enzymology*; D004950:Esterases / Q000032:analysis*; D005969:Glutamate Dehydrogenase / Q000032:analysis*; D007525:Isoelectric Focusing; D007770:L-Lactate Dehydrogenase / Q000032:analysis*; D008291:Malate Dehydrogenase / Q000032:analysis*; D013379:Substrate Specificity
D007770:L-Lactate Dehydrogenase; D008291:Malate Dehydrogenase; D005969:Glutamate Dehydrogenase; D004950:Esterases; D000135:Acid Phosphatase