Arrangement of glycan chains in the sacculus of Escherichia coli.
A novel of Escherichia coli endopeptidase was used for a selective partial hydrolysis of the peptide bridges which interlink the glycan chains in E. coli sacculi. The loosening of the murein network revealed, in the electron microscope, a preferential orientation of the glycan chains, more or less perpendicular to the length axis of the cell. Control incubations with E. coli transglycosylase or egg-white lysozyme did not leave ordered structures behind.
D004926:Escherichia coli / Q000032:analysis / Q000648:ultrastructure*; D009113:Muramidase; D010447:Peptide Hydrolases; D010457:Peptidoglycan; D011134:Polysaccharides / Q000032:analysis*; D011135:Polysaccharides, Bacterial / Q000032:analysis*; D014166:Transferases
D010457:Peptidoglycan; D011134:Polysaccharides; D011135:Polysaccharides, Bacterial; D014166:Transferases; D009113:Muramidase; D010447:Peptide Hydrolases