| Literature DB >> 2877048 |
P García, E García, C Ronda, R Lopez, R Z Jiang, A Tomasz.
Abstract
Two mutants of Streptococcus pneumoniae deficient in autolysin activity produced a protein that showed immunological identity with the N-acetyl-muramyl-L-alanyl-amidase present in the wild-type strain, when tested with antiserum obtained against this enzyme. The protein was produced by the mutant cultures grown either at 37 degrees C or at 30 degrees C, although only the cell extracts obtained at 30 degrees C showed significant cell wall hydrolysing activity. In contrast to the lysis resistance of these bacteria grown at 37 degrees C, mutant cultures grown at 30 degrees C exhibited significant degrees of autolysis when treated with detergent or cell wall inhibitors. Extracts of the mutant cultures contained a cell wall hydrolysing activity that was rapidly inactivated during incubation at 37 degrees C.Entities:
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Year: 1986 PMID: 2877048 DOI: 10.1099/00221287-132-5-1401
Source DB: PubMed Journal: J Gen Microbiol ISSN: 0022-1287