Characterization of a small proteolytic enzyme which lyses bacterial cell walls.
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.
D000418:Albumins; D001173:Arthrobacter / Q000201:enzymology*; D002364:Caseins; D002473:Cell Wall; D002850:Chromatography, Gel; D004586:Electrophoresis; D066298:In Vitro Techniques; D008970:Molecular Weight; D010447:Peptide Hydrolases; D014461:Ultracentrifugation
D000418:Albumins; D002364:Caseins; D010447:Peptide Hydrolases