The lytic enzyme present in 0C2(W) lysates was isolated by means of ion-exchange chromatography and further purified by gel filtration and ultrafiltration. The phage enzyme had an apparent pH optimum of 6 -5-6 -9 and was rapidly inactivated at temperatures > 47 °C. The apparent temperature optimum was 37 °C and Q 10 and E a values over the range 22-32 °C were 2-5 and 692 kJ/mol respectively. Monovalent and divalent cations activated the enzyme. Reduced -SH groups on the enzyme were required for lytic activity. Gel filtration revealed a mol. wt of ~ 46000. Strain-dependent differences in sensitivity of group N lactic streptococci to lysin were found. Group D streptococci were also lysed. Strains of three species of Leuconostoc, two species of Lactobacillus, one strain of Escherichia coli and of Micrococcus lysodeikticus were apparently resistant. Analysis of cell wall degradation products gave results which were consistent with the lysin having the specificity of an N-acetylmuramidase.The presence of phage-induced cell wall or capsule-dissolving (lytic) enzymes in lysates of phage-infected bacteria has been described for Escherichia coli, Staphylococcus aureus, Azotobacter agilis, Aerobacter cloacae, Bacillus megaterium, Micrococcus lysodeikticus, Bacillus stearothermophilus, Klebsiellapneumoniae, Pseudomonas putida, Ps. aeruginosa and for streptococcal phage-host systems (for a review see Tsugita, 1971). However, relatively little information is available for lactic streptococcal phage-associated lysins. Pette (1953) established that phage lysins had a broader lytic range than phage. Naylor & Czulak (1956) confirmed this finding and also found that lysins were more heat labile than phage. Oram & Reiter (1965) reported the partial purification of a lytic enzyme from phage (0ML3) lysates of Streptococcus lactis ML3. Unlike some other phage associated lysins, which lysed only damaged cells or viable cells sensitized by phage (e.g. Ralston et al. 1957;Murphy, 1961), the 0ML3 enzyme lysed viable cells of all strains of lactic streptococci tested. The enzyme was activated by cations and was classified as a muramidase. Tourville & Tokuda (1967) have also described the partial purification and characterization of a lytic enzyme derived from a ^ClO lysate of Str. lactis CIO. This enzyme reacted to cations in a manner similar to the 0ML3 lysin but differed in several respects including activation energy. Both groups noted that strain-dependent differences in sensitivity to phage lysin existed • Present address: Northern