Abstract
Salmonella typhi infected with Vi-phage II produce an enzyme dissolving chloroform-killed, gram-negative bacteria. The enzyme was purified 200 times by chromatography on Amberlite IRC 50. The specificity of its action was investigated using Micrococcus lysodeiktious cells, S. typhi murein and muropeptide C3. It has been shown that the enzyme splits off the cross-linking peptide bond between the amino group of diaminopimelic acid and the carboxyl group of alanine.
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