Characterization of a Small Proteolytic Enzyme Which Lyses Bacterial Cell Walls
- 1 February 1966
- journal article
- research article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 91 (2) , 524-+
- https://doi.org/10.1128/jb.91.2.524-534.1966
Abstract
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 glycosamino-peptide.This publication has 23 references indexed in Scilit:
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