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J. Biochem, 1981, Vol. 89, No. 1 275-284
© 1981 Japanese Biochemical Society

research-article

Lytic Enzyme Produced by Pseudomonas aeruginosa Concomitantly with Bacteriophage PS17. Purification, Characterization, and Comparison with PR1-Lysozyme

Hitoshi SAWADA, Masao AZEGAMI1 and Shin-ichi ISHII

Department of Biochemistry, Faculty of Pharmaceutical Sciences, Hokkaido University Kita-ku, Sapporo, Hokkaido 060
1 Deceased

A bacteriolytic enzyme was found to be produced, concomitantly with the progeny phage, in Pseudomonas aeruginosa P14 infected with phage PS17. The enzyme, named PS17-lysozyme, was purified by acrinol treatment, two cycles of Amberlite CG-50 chromatography, and SP-Sephadex C-50 chromatography. Homogeneity of the preparation was demonstrated by three electrophoretic techniques. PS17-lysozyme behaved like a basic protein (pl, 9–10) consisting of a single polypeptide chain (molecular weight, 24,500) and showed the substrate specificity of an N-acetyl-muramidase, i.e., the same specificity as hen egg-white lysozyme. The enzyme exhibited much higher specific activity than the egg-white enzyme when assayed with chloroform-killed P. aeruginosa P14 as a substrate. These characteristics, as well as the amino acid composition, were very similar to those of PR1-lysozyme; a bacteriolytic enzyme produced in mitomycin C-induced P. aeruginosa P15 concomitantly with a phage-tail-like bacteriocin, pyocin RI (Ochi et al. (1978) J. Biochem. 83, 727–736). However, the behavior of these two lysozymes from P. aeruginosa in Amberlite CG-50 chromatography and some other properties indicated that they were not identical, though they were similar. The results are in accord with the view that pyocin RI may be a defective form of a bacteriophage closely related to but not identical with phage PS17.


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