Kleppe G, Vasstrand E, Jensen H B
Eur J Biochem. 1981 Oct;119(3):589-93. doi: 10.1111/j.1432-1033.1981.tb05648.x.
Bacillus cereus peptidoglycan with N-unsubstituted glucosamine residues was insensitive to treatment with bacteriophage T4 lysozyme. After N-acetylation with acetic anhydride, T4 lysozyme cleared solutions of the peptidoglycan and reducing sugars were liberated. The digestion products were mainly of high molecular weight, since the peptidoglycan is peptide cross-linked to a great extent. N-Propylation did not convert the partially N-unsubstituted peptidoglycan to a sensitive form. It is concluded that the acetamido groups are required for binding and/or catalysis by T4 lysozyme.
含有N-未取代葡糖胺残基的蜡样芽孢杆菌肽聚糖对噬菌体T4溶菌酶处理不敏感。用乙酸酐进行N-乙酰化后,T4溶菌酶使肽聚糖溶液变清并释放出还原糖。消化产物主要是高分子量的,因为肽聚糖在很大程度上是通过肽交联的。N-丙基化并未将部分N-未取代的肽聚糖转变为敏感形式。得出的结论是,乙酰氨基基团是T4溶菌酶结合和/或催化所必需的。