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

@article{Doughty1967PurificationAP,
  title={Purification and properties of a bacteriophage-induced cell wall peptidase from Staphylococcus aureus.},
  author={C C Doughty and Jeffrey A Mann},
  journal={Journal of bacteriology},
  year={1967},
  volume={93 3},
  pages={1089-95}
}
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… CONTINUE READING
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Referenced Papers

Publications referenced by this paper.
Showing 1-4 of 4 references

Structure of the cell wall of Staphylococcus aureus strain Copenhagen . VI . The soluble glycopeptide and its sequential degradation by peptidases

  • B. S. BAER, AND A. P. KRUEGER
  • Biochemistry
  • 1965

Virolysin , a phage induced lysin

  • AND M. McIvoR
  • J . Gen . Microbiol .
  • 1961

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