Springer Online Journal Archives 1860-2000
Abstract Antibody to purified glutamine synthetase from Escherichia coli was prepared and used for an immunological comparison of glutamine synthetases from species of Salmonella, Citrobacter, Enterobacter, Serratia, Proteus, Erwinia, Aeromonas, Pseudomonas, Acinetobacter, Xanthomonas, Alcaligenes, and Paracoccus. The results of Ouchterlony double diffusion experiments and quantitative microcomplement fixation studies indicated that the amino acid sequence of this enzyme was highly conserved in different organisms. The order of relationship to E. coli was found to be similar to that derived from immunological investigations of other enzymes. In addition, congruence was observed between ribosomal RNA homology and the results of the microcomplement fixation experiments. The results also suggested that some species of Alcaligenes were more closely related to species of Pseudomonas than to each other. Immunological comparisons of glutamine synthetases appear to be very useful for the elucidation of relationships among distantly related species and genera.
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