Summary: Four of the five penicillin-binding proteins in the cytoplasmic membranes of have been purified to protein homogeneity. The method used involved the solubilization of the penicillin-binding proteins from the membranes by treatment with non-ionic detergent, followed by partial separation of the proteins by ion-exchange chromatography on DEAE-Sepharose CL-6B. Each protein was then purified to protein homogeneity by covalent affinity chromatography on ampicillin–affinose. The protein with the lowest molecular weight is a -carboxypeptidase. The other three proteins have previously been postulated to be peptidoglycan transpeptidases, endopeptidases or -carboxypeptidases , but it was not possible to demonstrate any of these activities with the purified proteins in various systems. Possible reasons for the observed lack of enzymic activity are discussed.


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