@article{mbs:/content/journal/micro/10.1099/00221287-114-2-349, author = "Williamson, Russell and Ward, J. Barrie", title = "Characterization of the Autolytic Enzymes of Clostridium perfringens", journal= "Microbiology", year = "1979", volume = "114", number = "2", pages = "349-354", doi = "https://doi.org/10.1099/00221287-114-2-349", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-114-2-349", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", abstract = " Clostridium perfringens and isolated walls of this organism autolysed rapidly when incubated in buffer at pH 7·0 with the release of free-reducing groups but no N-terminal amino acids. The predominant autolytic enzyme was an endo-β-N-acetylglucosaminidase, and an endo-β-N-acetylmuramidase was also present. The autolytic enzymes could be solubilized by extraction of the organisms with 5 m-LiC1 and would then subsequently bind to and rapidly lyse walls of Micrococcus luteus and, more slowly, formamide-extracted walls of C. perfringens and walls of Bacillus subtilis. Lysis of C. perfringens walls by these extracted enzymes could not be demonstrated.", }