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Journal of Bacteriology logoLink to Journal of Bacteriology
. 1974 Feb;117(2):796–804. doi: 10.1128/jb.117.2.796-804.1974

Specificity of the Autolysin of Streptococcus (Diplococcus) pneumoniae

Lawrence V Howard a,1, Harry Gooder a
PMCID: PMC285575  PMID: 4149515

Abstract

A Streptococcus (Diplococcus) pneumoniae autolysin, partially purified from cellular autolysates, was optimally active at pH 7.0 and was stimulated by monovalent cations. Addition of autolysin to walls resulted in the appearance of only N-terminal l-alanine, whereas no glycosidase activity was observed. Walls which had been solubilized by autolysin were separated by gel filtration into a low-molecular-weight peptide containing amino acids in the same ratios found in intact walls and a high molecular fraction containing the amino acid-deficient peptidoglycan backbone. Thus, the major activity is an N-acetylmuramyl-l-alanine amidase. In addition, walls undergoing spontaneous lysis revealed no glycosidase activity but showed an increase in only N-terminal alanine. Autolysin, which was bound to walls in saline, was almost completely removed when walls were washed in distilled water, and all of the activity was recovered in the water wash fluid.

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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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