[Immunological study of glyceraldehyde-3-phosphate dehydrogenase in Enterobacteriaceae; taxonomic value].
The antigenic structure of glyceraldehyde-3-phosphate dehydrogenase of the most representative Enterobacteriaceae species were compared with an antiserum to Escherichia coli glyceraldehyde-3-phosphate dehydrogenase. The results of the immunodiffusion experiments were confirmed and specified by micro-complement fixation studies. They demonstrated a total immunological identity between the E. coli enzyme and the enzymes of Alcalescens-dispar and the Shigella species, a marked relatedness of the Salmonella species enzyme and a more or less significant relation of the enzymes of the other Enterobacteriaceae species. Moreover, the micro-complement fixation had the same sensitivity and a better selectivity than the DNA/DNA hybridizations. The results show that, like DNA polymerase, this enzyme has evolved more slowly than the other enzymes studied at this time.
D003168:Complement Fixation Tests; D004755:Enterobacteriaceae / Q000145:classification / Q000201:enzymology*; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000276:immunology*; D005779:Immunodiffusion; D007122:Immunoelectrophoresis
D005987:Glyceraldehyde-3-Phosphate Dehydrogenases
Etude immunologique de la glycéraldéhyde-3-phosphate-déshydrogénase chez les Entérobactéries; intérêt taxonomique.