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- W1966605838 abstract "In order to obtain a lysozyme substrate which can be assayed colorimetrically, p-nitrophenyl-O-(2-acetamido-2-deoxy-β-D-glucopyranosyl)-(1 → 4)-O-(2-acetamido-2- deoxy-β-D-glucopyranosyl)-(1 → 4)-2-acetamido-2-deoxy-β-D-glucopyranoside was synthesized. The action of egg-white lysozyme (N-acetylmuramide glycanohydrolase, EC 3.2.1.17) on this compound was found to be random, hydrolysis occurring by two pathways, namely one which liberates p-nitrophenol and another which liberates p-nitrophenyl-2-acetamido-2-deoxy-β-D-glucopyranoside. The reaction of the substrate with lysozyme was inhibited non-competitively by N,N-diacetylchitobiose or N-acetyllactosamine, whereas N,N,N-triacetylchitotriose inhibited the reaction competitively. These results suggest that at least three monosaccharide units are necessary for binding to the active site of lysozyme." @default.
- W1966605838 created "2016-06-24" @default.
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- W1966605838 date "1966-11-01" @default.
- W1966605838 modified "2023-10-11" @default.
- W1966605838 title "Lysozyme substrates. Chemical synthesis of p-nitrophenyl O-(2-acetamido-2-deoxy-β-D-glucopyranosyl)-(1 → 4)- 2-acetamido-2-deoxy-β-D-glucopyranoside and its reaction with lysozyme" @default.
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- W1966605838 doi "https://doi.org/10.1016/0304-4165(66)90008-0" @default.
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