| Literature DB >> 3938476 |
Abstract
Muramidase digests of alkali-treated SDS-insoluble peptidoglycan from two strains of Neisseria gonorrhoeae were examined. Both strains contained disaccharide peptide monomers that had intramolecular 1,6-anhydro-muramyl ends. In contrast to strain 1L260, in which 50% of the monomer fraction is O-acetylated, the monomer fraction from strain RD5 was completely devoid of O-acetyl groups, as shown by HPLC. Penicillin decreased the O-acetylation of peptidoglycan but did not affect the proportion of anhydro-muramyl residues.Entities:
Mesh:
Substances:
Year: 1985 PMID: 3938476 DOI: 10.1099/00221287-131-12-3397
Source DB: PubMed Journal: J Gen Microbiol ISSN: 0022-1287