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. 1969 Mar;97(3):1310–1320. doi: 10.1128/jb.97.3.1310-1320.1969

Immunochemical and Enzymatic Comparisons of the Tryptophan Synthase α Subunits from Five Species of Enterobacteriaceae

T M Murphy 1, S E Mills 1
PMCID: PMC249849  PMID: 4887511

Abstract

The reactive surface structures of α subunits of tryptophan synthase from Escherichia coli, Shigella dysenteriae, Salmonella typhimurium, Aerobacter aerogenes, and Serratia marcescens were compared by measuring (i) their reactivities in micro-complement-fixation assays with antibodies directed specifically to E. coli wild-type α subunit, (ii) their reactivities in enzyme neutralization assays with the same antibodies, and (iii) their binding affinities for tryptophan synthase β2 subunits. The enzymes from the four heterologous species cross-reacted in the microcomplement-fixation assays with the anti-E. coli α subunit antibodies, each to a different degree. However, neutralization titers of the antibodies reacting with the various α subunits were comparatively similar, and the β2 subunit-binding and -stimulating abilities of the α subunits were even more closely alike. The results suggested that the tertiary structure of the β2 subunit-binding site of the α subunit has been conserved, relative to the rest of the molecule, during the evolutionary divergence of the species of Enterobacteriaceae.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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