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Journal of Antimicrobial Chemotherapy (1987) 19, 743-751
© 1987 The British Society for Antimicrobial Chemotherapy

research-article

Inhibition of Providencia stuartii cell envelope enzymes by chlorhexidine

Ian Chopra, Susan C. Johnson and Peter M. Bennett

Department of Microbiology, The Medical School, University of Bristol Bristol BS8 1TD, England

accepted 16 December 1986

The possibility that chlorhexidine is a specific inhibitor of membrane bound bacterial adenosine triphosphatase (ATPase) was addressed. The in-vitro susceptibilities of several Providencia stuartii cell envelope enzymes, including ATPase, to chlorhexidine were compared. The following concentrations of chlorhexidine were required to cause 50% inhibition of enzyme activity in preparations from chlorhexidine-sensitive strains (MIC 50 mg chlorhexidine/l): ATPase (160 mg/1), succinic dehydrogenase (> 300.mg/1), penicillin binding protein 7 (300 mg/l) and ß-lactamase (45 mg/1). Fifty per cent inhibition of the ATPase from a chlorhexidine-resistant strain (MIC 1600 mg/1) was achieved at an in-vitro concentration of 225 mg chlorhexidine/l. Our observations do not support the suggestion that bacterial membrane-bound ATPases are specific targets for chlorhexidine.


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