Mirelman D, Kleppe G, Jensen H B
Eur J Biochem. 1975 Jul 1;55(2):369--3. doi: 10.1111/j.1432-1033.1975.tb02171.x.
Lysozyme from bacteriophage T4 was found to digest a soluble, uncrosslinked peptidoglycan which is secreted by cells of Micrococcus luteus when incubated in the presence of penicillin G. Analysis of the enzymatic degradation products shows that T4 acts as an endo-acetylmuramidase capable of cleaving glycosidic bonds only at muramic acid residues that are substituted with peptide side-chains. The results indicate that the secreted peptidoglycan may consist of a mixture of chains, approximately half of which are substituted by peptide side chains on most of their muramic acid residues, while the other half is made up of chains in which the muramic acid moieties are unsubstituted.
人们发现，来自噬菌体T4的溶菌酶能够消化一种可溶的、未交联的肽聚糖，这种肽聚糖是在青霉素G存在的情况下，由藤黄微球菌细胞分泌的。对酶促降解产物的分析表明，T4作为一种内切乙酰胞壁酸酶，仅能在被肽侧链取代的胞壁酸残基处切割糖苷键。结果表明，分泌的肽聚糖可能由链的混合物组成，其中大约一半的链在其大部分胞壁酸残基上被肽侧链取代，而另一半则由胞壁酸部分未被取代的链组成。
