Abstract
Peptides from partial acid hydrolysates of purified mucopeptide from Aerobacter cloacae NRC 492 were isolated by a combination of high-voltage paper electrophoresis and paper chromatography. Three dipeptides (L-ala.D-glu, D-glu.meso-Dap, and meso-Dap.D-ala), two tripeptides (ala.D-glu.meso-Dap and D-glu.meso-Dap.ala, i.e. D-glutamyl.meso-diaminopimelyl.alanine), and a tetrapeptide were partially characterized. Molar ratios, sequence, and optical configurations in a tripeptide from the wall corresponded with those in a uridine diphospho muramyl tripeptide from penicillin-treated cells of the same organism and with those of a tripeptide synthesized in vitro by enzymes from cell sonicates.
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