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J Bacteriol. 1967 March; 93(3): 1089-1095
Copyright © 1967 American Society for Microbiology. All Rights Reserved.

Purification and Properties of a Bacteriophage-induced Cell Wall Peptidase from Staphylococcus aureus

Department of Preventive Medicine, University of Illinois College of Medicine, Chicago, Illinois
Department of Biological Chemistry, University of Illinois College of Medicine, Chicago, Illinois

ABSTRACT

A phage-induced cell wall solubilizing enzyme isolated from phage-infected Staphylococcus aureus phage type 80 was purified 588-fold. The pH optimal activity was 6.8 to 7.3, and pH optimal stability, 6.5 to 7.5. It was inhibited by p-hydroxymercuribenzoate, ethylenediaminetetraacetic acid, and specific rabbit antisera. The cell wall lytic reaction is a peptidase resulting in cleavage of the cell wall peptide at N-terminal alanine, glutamic acid, and glycine. Electron micrographs are shown of cell wall "ghosts" remaining after the enzymatic digestion of cell walls.