Characterization of a Small Proteolytic Enzyme Which Lyses Bacterial Cell Walls

Abstract

Ensign , J. C. (University of Wisconsin, Madison), and R. S. Wolfe . Characterization of a small proteolytic enzyme which lyses bacterial cell walls. J. Bacteriol. 91: 524–534. 1966.—An enzyme isolated from a myxobacter possesses both cell-wall lytic and proteolytic activity. The enzyme has been purified over 600-fold and is electrophoretically homogeneous upon cellulose acetate at several p H values and upon polyacrylamide gel columns. A single peak was obtained upon ultracentrifugation and density gradient centrifugation. Based upon Sephadex gel filtration, a molecular weight of 8,700 was determined for the enzyme. Albumin and casein were extensively degraded by the enzyme, with approximately one-third of the peptide bonds present in these proteins being hydrolyzed. The enzyme lyses cell walls by hydrolyzing peptide bonds in the glycosaminopeptide.