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. 1967 Mar;93(3):1089-95.
doi: 10.1128/jb.93.3.1089-1095.1967.

Purification and properties of a bacteriophage-induced cell wall peptidase from Staphylococcus aureus

C C Doughty, J A Mann

Purification and properties of a bacteriophage-induced cell wall peptidase from Staphylococcus aureus

C C Doughty et al. J Bacteriol. 1967 Mar.

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.

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