Arrangement of glycan chains in the sacculus of Escherichia coli.
AUTOR(ES)
Verwer, R W
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=218599Documentos Relacionados
- Elasticity of the sacculus of Escherichia coli.
- The respiratory chains of Escherichia coli.
- Molecular model for elongation of the murein sacculus of Escherichia coli.
- Heterogeneity of newly inserted and preexisting murein in the sacculus of Escherichia coli.
- Generation of antibody activity from immunoglobulin polypeptide chains produced in Escherichia coli.