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. 1979 Jan;137(1):474–479. doi: 10.1128/jb.137.1.474-479.1979

Penicillin-binding proteins in Proteus species.

S Ohya, M Yamazaki, S Sugawara, M Matsuhashi
PMCID: PMC218473  PMID: 368025

Abstract

Penicillin-binding proteins in three species of Proteus, Proteus mirabilis, P. morganii, and P. rettgeri, were investigated by sodium dodecyl sulfate-polyacrylamide slab gel electrophoresis. Penicillin-binding proteins in these Proteus species were compared with those in Escherichia coli K-12. An approximate correlation between penicillin-binding proteins in E. coli and those in Proteus species was shown by several criteria: electrophoretic mobilities; affinities of several beta-lactam antibiotics which show characteristic patterns of binding to penicillin-binding proteins in E. coli; relation between affinities of antibiotics to the proteins and effects on morphological changes in Proteus species; location of beta-lactamase activity among penicillin-binding proteins; and thermostability. The electrophoretic mobilities and several other characteristics of penicillin-binding proteins among the Proteus species examined were found to be similar from species to species and differed only slightly from those of E. coli.

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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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