Isolation and properties of car☐ylesterase P4 from Yersinia Pseudotuberculosis

FEMS Microbiology Reviews

1995

The specific activities of esterases and certain other molecular properties including immunospecificity indicate that the electrophoretic variations of these enzymes in bacterial populations are the result of allelic variations at specific gene loci. The esterase polymorphism of Enterobacteriaceae and some other species isolated from man or animals demonstrates that esterases can distinguish between bacteria at the species or subspecies level, both by their biochemical properties and by their electrophoretic differences. The esterase data complement DNA hybridization studies and agree with ribosomal DNA polymorphism, especially for delineating a phylogenetically distinct group of highly pathogenic strains in Escherichia coli. A two‐dimensional electrophoretic profile obtained by establishing a direct correspondence between homologous esterase bands resolved by independent runs of isoelectric focusing and standard electrophoresis considerably improves the detection of allelic variations, whereas protein titration curves (electrophoresis in pH gradient) can be used to demonstrate the real electrophoretic homogeneity of allozymes or evalue their molecular relationship in terms of apparent amino acid substitutions. This overview establishes that esterases, by their significant electrophoretic polymorphism, are reliable molecular markers for systematics and epidemiology, and are suitable enzyme systems for studying population genetics and phylogeny.

Section: Purified Esterasesmentioning

confidence: 99%

Section: Purified Esterasesmentioning

confidence: 99%

Section: Yersiniumentioning

confidence: 99%

Section: Yersiniumentioning

confidence: 99%

See 2 more Smart Citations

The electrophoretic polymorphism of bacterial esterases

FEMS Microbiology Reviews

1995

“…Y. pseudotuberculosis differs from Y enterocolitica by the presence of EST P4, a slow migrating major S/a-EST, and by the absence of EST E,, a thermostable R/@-EST [60,64,131]. The EST Pa of Y. pseudotuberculosis and the EST P4 of Y. pestis are identical in terms of physicochemical and biochemical properties and immunospecificity [77]. These findings agree with the similarity between the DNA of the two organisms [I321 and substantiate their taxonomic relatedness.…”

Section: Yersiniumentioning

confidence: 99%

The electrophoretic polymorphism of bacterial esterases

FEMS Microbiology Reviews

1995

The spectic activities of esterases and certain other molecular properties including immunospecificity indicate that the electrophoretic variations of these enzymes in bacterial populations are the result of allelic variations at specific gene loci. The esterase polymorphism of Enterobacteriaceae and some other species isolated from man or animals demonstrates that esterases can distinguish between bacteria at the species or subspecies level, both by their biochemical properties and by their electrophoretic differences. The esterase data complement DNA hybridization studies and agree with ribosomal DNA polymorphism, especially for delineating a phylogenetically distinct group of highly pathogenic strains in Escherichia coli. A two-dimensional electrophoretic profile obtained by establishing a direct correspondence between homologous esterase bands resolved by independent runs of isoelectric focusing and standard electrophoresis considerably improves the detection of allelic variations, whereas protein titration curves (electrophoresis in pH gradient) can be used to demonstrate the real electrophoretic homogeneity of allozymes or evalue their molecular relationship in terms of apparent amino acid substitutions. This overview establishes that esterases, by their significant electrophoretic polymorphism, are reliable molecular markers for systematics and epidemiology, and are suitable enzyme systems for studying population genetics and phylogeny.

Characterization of Enterobacteria by Esterase Specific-Activity Profiles

Journal of General Microbiology

1990

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The spectrum of specific activities and the electrophoretic mobilities of esterases produced by 550 strains of Enterobacteriaceae belonging to 36 species and subclassified into six groups (group 1, Escherichia cofi, Shi'geflu and Escherichia hermanii; group 2, genus Sizfmoneffa and genus Citrobacter; group 3, genus Kfebsieffa and genus Enterobacter; group 4, genus Serrutiu and Serratia fonticolu; group 5, genus Proteus, genus Protridenct'a and genus Motgunelfa; and group 6, genus Yersiniu) were analysed by acrylamide/agarose gel electrophoresis using standardized methods for staining and mobility comparisons. Nineteen types of esterase were defined by their respective esterase specific-activity profile (ESAP). A multiple correspondence analysis (MCA) of the ESAP data enabled 82% of the strains in the 36 species to be correctly classified. In each group, the species were clearly delineated after MCA on both ESAP and electrophoretic mobility data. In addition, the smallest number of characters pro9ding species identification of Yersinia strains by esterase polymorphism was identified by means of a binary segmentation tree technique.