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J Bacteriol. 1969 April; 98(1): 182-189
Copyright © 1969 American Society for Microbiology. All Rights Reserved.

Effect of Lytic Enzymes of Acanthamoeba castellanii on Bacterial Cell Walls

Spencer Rosenthal, Elizabeth J. Reed and Robert A. Weisman1

a Department of Biochemistry, Woman's Medical College of Pennsylvania, Philadelphia, Pennsylvania 19129

ABSTRACT

Extracts of Acanthamoeba castellanii (Neff) contain {alpha}- and ß-glucosidase, ß-galactosidase, ß-N-acetylglucosaminidase, amylase, and peptidase. All of these activities are optimal between pH 3 and 4. These extracts also were found to clarify suspensions of cell walls from nine different gram-positive bacteria, including Micrococcus lysodeikticus. The pH optimum for the lytic activity was between 3 and 4. The extent of lysis of the various cell walls did not correlate with the release of free amino groups and of free N-acetylated sugars from the walls during digestion with these extracts. Suspensions of cell walls of Escherichia coli (a gram-negative bacterium), Cordiceps militaris (a fungus), and Acanthamoeba cysts, as well as of colloidal chitin, were not clarified by incubation with these extracts, although reducing sugars were released from each of these materials. Exhaustive digestion of M. lysodeikticus walls by lysozyme released no free N-acetylglucosamine. The products of exhaustive digestion of this cell wall with Acanthamoeba extracts were free N-acetylglucosamine, free N-acetylmuramic acid, glycine, alanine, glutamic acid, lysine, and N-acetylmuramic acid peptide fragments. These results suggest that the amoeba extracts contain endo- and exo-hexosaminidases, in addition to ß-hexosaminidase and peptide hydrolases.

FOOTNOTES

1 Present address: Department of Biochemistry, University of Texas Medical School, San Antonio, Tex.

J Bacteriol. 1969 April; 98(1): 182-189
Copyright © 1969 American Society for Microbiology. All Rights Reserved.



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