Penicillin-binding proteins in Proteus species.
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.
D001426:Bacterial Proteins / Q000032:analysis*; D002352:Carrier Proteins / Q000032:analysis*; D002511:Cephalosporins / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006358:Hot Temperature; D010400:Penicillin G / Q000378:metabolism; D010406:Penicillins / Q000378:metabolism; D011511:Proteus / Q000032:analysis*; D011513:Proteus mirabilis / Q000032:analysis*; D013045:Species Specificity; D001618:beta-Lactamases / Q000032:analysis
D001426:Bacterial Proteins; D002352:Carrier Proteins; D002511:Cephalosporins; D010406:Penicillins; D001618:beta-Lactamases; D010400:Penicillin G