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- W1487692013 abstract "Cell walls of Arthrobacter crystallopoietes grown as spheres and as rods were solubilized by treatment with the B enzyme from Chalaropsis , an N -acetylmuramidase. The neutral glycopeptides were then isolated by chromatography on ECTEOLA cellulose. The glycopeptides, consisting of disaccharide-peptide units interlinked by peptide cross-bridges, were fractionated by gel filtration on Sephadex columns into oligomers of various sizes. The size distribution ranged from monomers with no cross-bridges to polymers with a high degree of polymerization, but did not differ significantly between cell walls from cells grown as spheres or rods. Some small differences in the distribution of C- and N-terminal amino acids were found. Analyses revealed that all the peptide bridges in the glycopeptide fractions from rod cell walls were formed by one l -alanine residue. In sphere cell walls, l -alanine was also found, but, in addition, higher oligomers of the glycopeptide contained glycine in their cross-bridges. These results were confirmed by determinations of C- and N-terminal amino acids released after lysostaphin and AL-1 enzyme digestions and by Edman degradations. Models representing the structures of the sphere and rod cell walls are presented. These structures indicate that the sphere cell wall is probably a more loosely knit macromolecule than is the rod cell wall." @default.
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- W1487692013 date "1967-09-01" @default.
- W1487692013 modified "2023-09-27" @default.
- W1487692013 title "Sphere-Rod Morphogenesis in <i>Arthrobacter crystallopoietes</i> II. Peptides of the Cell Wall Peptidoglycan" @default.
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- W1487692013 doi "https://doi.org/10.1128/jb.94.3.741-750.1967" @default.
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