@article{mbs:/content/journal/micro/10.1099/00221287-129-2-489, author = "Garcia, Pedro and Garcia, Ernesto and Ronda, Concepcion and Lopez, Rubens and Tomasz, Alexander", title = "A Phage-associated Murein Hydrolase in Streptococcus pneumoniae Infected with Bacteriophage Dp-1", journal= "Microbiology", year = "1983", volume = "129", number = "2", pages = "489-497", doi = "https://doi.org/10.1099/00221287-129-2-489", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-129-2-489", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", abstract = "A phage-associated murein hydrolase activity capable of degrading pneumococcal cell walls was isolated and purified to homogeneity from the phage-induced lysate of an autolysis-defective pneumococcal mutant infected with the bacteriophage Dp-1. Some properties of the enzyme resembled those of the wild-type (host) pneumococcal murein hydrolase: cell walls prepared from ethanolamine-grown pneumococci were resistant to the enzyme; the activity was inhibited by the Forssman antigen and was sensitive to proteolytic enzymes. The phage-associated enzyme was not inhibited by antiserum prepared against the purified pneumococcal murein hydrolase; the activity was stimulated by reducing agents and was partially inhibited by cardiolipin. The subunit molecular weight of the phage-associated enzyme was somewhat smaller (31000) than that of the pneumococcal hydrolase (35000). This appears to be the first description of a phage-associated murein hydrolase activity in pneumococci.", }