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- W1567863666 abstract "A phage-induced cell wall solubilizing enzyme isolated from phage-infected Staphylococcus aureus phage type 80 was purified 588-fold. The p H optimal activity was 6.8 to 7.3, and p H 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." @default.
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- W1567863666 date "1967-03-01" @default.
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- W1567863666 title "Purification and Properties of a Bacteriophage-induced Cell Wall Peptidase from <i>Staphylococcus aureus</i>" @default.
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- W1567863666 doi "https://doi.org/10.1128/jb.93.3.1089-1095.1967" @default.
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