Purification and Some Properties of Bacteriophage T4 Particle‐Associated Lysozyme

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Abstract
Bacteriophage T4 particle‐associated lysozyme, purified to electrophoretic homogeneity, was found to be a protein with a relative molecular mass of 15000. The lysozyme was purified from the particles of bacteriophage T4 e mutant and from the lysates of the 5tsl e T4 mutant, in which the enzyme is in soluble form. In the purification procedure advantage was taken of the affinity of the enzyme for GlcNAc‐MurNac‐LAla‐DGlu‐msA2pm‐DAl a (C6 muropeptide), one of the product of the digestion of Escherichia coli murein with lysozyme. The test for the quick estimation of bacteriolytic activity of the enzyme, using E. coli B freeze‐dried cells, is described. The pH optimum of the particle‐associated lysozyme was equal to about 6.0, ionic strength optimum to 0.05–0.1 M, and optimum Triton X‐100 concentration to 1%, when this substrate was used. Some of the aspects of the possible biological significance of the particle‐associated lysozyme in bacteriophage T4 infection are discussed.