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. 1966 Feb;91(2):524–534. doi: 10.1128/jb.91.2.524-534.1966

Characterization of a Small Proteolytic Enzyme Which Lyses Bacterial Cell Walls

J C Ensign 1, R S Wolfe 2
PMCID: PMC314891  PMID: 5935339

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 pH 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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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