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

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.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Doughty CC,Mann JA

doi

10.1128/JB.93.3.1089-1095.1967

subject

Has Abstract

pub_date

1967-03-01 00:00:00

pages

1089-95

issue

3

eissn

0021-9193

issn

1098-5530

journal_volume

93

pub_type

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