Abstract
Free di-saccharide (N-acetylglucosamine-N-acetylmuramic acid) is released from a purified amino sugar complex, probably tetra-saccharide, by the action of egg-white lysozyme and of a similar enzyme secreted by a Streptomyces. The di-saccharide is also released from a purified poly-acetylamino sugar-peptide-di-saccharide compound by the action of the same enzymes on its poly-acetylamino sugar moiety. Differences in the affinity of egg-white lysozyme and of the Streptomyces enzyme for their substrates are discussed. A second bacteriolytic enzyme, also secreted by the Streptomyces, liberates free disaccharide from the purified peptide-di-saccharide and poly-acetylamino sugar-peptide-di-saccharide complexes by splitting the bond between the carboxyl group of muramic acid and the amino group of the peptide moiety.
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