SUMMARY: A lytic enzyme was isolated and purified from PL-1 phage-induced lysates of the host ATCC 27092. The molecular weight of the enzyme was about 30000. Maximum activity on the lysis of the host cell walls occurred at pH 6.0-6.5 and at 45 °C. The enzyme activity was inhibited by heavy metal ions, SH- and serine-enzyme inhibitors and -phenanthroline. The reducing end of the enzymic digest was muramic acid and the enzyme was considered to be an endo--acetylmuramidase. However, the enzyme differed from the other known -acetylmuramidases including hen's egg-white lysozyme in several enzymic properties.


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