Isolation and characterization of soluble peptidoglycan from several strains of Streptococcus faecium.
Two phenotypically autolysis-deficient strains of Streptococcus faecium ATCC 9790 were shown to produce high-molecular-weight, soluble, linear, uncross-linked peptidoglycan when incubated with benzylpenicillin in a wall medium which permits cell wall synthesis (wall thickening) but not balanced growth. This high-molecular-weight s-peptidoglycan was shown to have a molecular weight of 46,000 to 54,000, lack peptide cross-links, and be virtually devoid of accessory wall polymers. It was hydrolyzed by hen egg white lysozyme and the endogenous, autolytic N-acetylmuramidase of S. faecium, but was not attacked by proteinases. Chemical analyses of the polymer are consistent with the following structure, where n is the number of repeating disaccharide units: (formula; see text).
D000595:Amino Acid Sequence; D002240:Carbohydrate Sequence; D002250:Carbon Radioisotopes; D008970:Molecular Weight; D010457:Peptidoglycan / Q000302:isolation & purification*; D010641:Phenotype; D013045:Species Specificity; D013291:Streptococcus / Q000032:analysis*; D014316:Tritium
D002250:Carbon Radioisotopes; D010457:Peptidoglycan; D014316:Tritium