Purification and properties of lysozyme induced by wild and amber mutant colitis phage and from cloned gene

The colitis phage induces lysozyme 9 min after infection of host Escherichia coli B. An amber mutant of the phage, under nonpermissive conditions, gave apprximately 60% more lysozyme activity than that of wild-type phage. The increase in enzyme activity was due to an increase in the amount of lysozyme protein rather than the activation of the enzyme. Lysozymes from wild-type, amber mutant phage-infected cells, and cloned gene were purified to homogeneity, and the molecular weight was detected as 15,500. They had identical electrophoretic mobilities, immunological properties, and amino acid compounds. The phage and hen egg white lysozymes differed in their hydrophobicities and amino acid compounds. There was no immunological cross-reactivity between colitis phage lysozyme antibody and phage T4 lysozyme