Reference : The cell envelope in Proteus vulgaris P 18 : Isolation and characterization of the pe...
Scientific journals : Article
Life sciences : Microbiology
Life sciences : Biochemistry, biophysics & molecular biology
The cell envelope in Proteus vulgaris P 18 : Isolation and characterization of the peptidoglycan component
Fleck, J. [Université Louis Pasteur (Strasbourg) - ULP > Institut de Bactériologie > > >]
Mock, M. [Université Louis Pasteur (Strasbourg) - ULP > Institut de Bactériologie > > > >]
Minck, R. [Université Louis Pasteur (Strasbourg) - ULP > Institut de Bactériologie > > > >]
Ghuysen, Jean-Marie [Université de Liège - ULiège > Institut de Botanique > Service de Microbiologie > > > >]
Biochimica et Biophysica Acta. Biomembranes
Elsevier Science
Yes (verified by ORBi)
[en] agglutination tests ; amidohydrolases ; amino acids/analysis ; animals ; bacillus subtilis/enzymology ; carboxypeptidases ; cattle ; cell wall/*analysis ; chromatography gel ; chromatography ion exchange ; chromatography paper ; chromatography ; detergents ; disaccharides analysis ; electrophoresis paper ; epididymis enzymology ; glucosamine analysis ; glycosaminoglycans analysis ; hexosaminidases ; hot temperature ; immunodiffusion ; kinetics ; male ; microscopy electron ; mitosporic fungi enzymology ; muramidase ; pancreas enzymology ; peptide hydrolases pharmacology ; peptidoglycan analysis isolation & purification ; polysaccharides ; proteus cytology ; rabbits ; streptomyces enzymology ; sulfuric acids ; swine ; trypsin pharmacology ; thin layer ; bacterial analysis ; drug effects
[en] Degradation of heat-treated cells of Proteus vulgaris P 18 with a protease preparation from a soil Bacillus subtilis allowed the isolation of a cell envelope structural entity, 60-70 Å thick, consisting of two electron-dense layers separated by a light one and composed, at least in part, of lipopolysaccharide O-antigen and of peptidoglycan. An enriched preparation, of which 55 % of the dry weight consisted of an intact peptidoglycan, was obtained through the sequential action upon lyophilized cells of hot aqueous sodium dodecyl sulfate and B. subtilis protease.
Both Chalaropsis B endo-N-acetylmuramidase and Streptomyces DD carboxy-peptidase solubilized the enriched peptidoglycan preparation. The Chalaropsis enzyme completely degraded the glycan moiety into peptide-substituted disaccharide units. The DD carboxypeptidase hydrolyzed the D-alanyl-(D)-meso-diaminopimelic acid linkages involved in peptide cross-linking. In the intact peptidoglycan, about 35 % of the L-alanyl-γ-D-glutamyl-(L)-meso-diaminopimelic acid-(L)-D-alanine residues occurred as uncross-linked monomers, 40 % of them as peptide dimers and 16 % as peptide trimers. It is likely that not all the peptides retained the D-alanine residue at their C-termini. About half of the N-acetylmuramic acid residues in the glycan moiety are O-acetylated, a property which is compatible with the high lysozyme resistance exhibited by the P. vulgaris peptidoglycan.
Fonds de la Recherche Fondamentale
Researchers ; Professionals

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