| Literature DB >> 4225890 |
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.Entities:
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Year: 1967 PMID: 4225890 PMCID: PMC276557 DOI: 10.1128/jb.93.3.1089-1095.1967
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490