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Linear, uncross-linked peptidoglycan secreted by penicillin-treated Bacillus subtilis. Isolation and characterization as a substrate for penicillin-sensitive D-alanine carboxypeptidases.由青霉素处理的枯草芽孢杆菌分泌的线性、未交联肽聚糖。作为青霉素敏感的D-丙氨酸羧肽酶底物的分离与特性鉴定。
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从多株粪肠球菌中分离并鉴定可溶性肽聚糖。

Isolation and characterization of soluble peptidoglycan from several strains of Streptococcus faecium.

作者信息

Barrett J F, Shockman G D

出版信息

J Bacteriol. 1984 Aug;159(2):511-9. doi: 10.1128/jb.159.2.511-519.1984.

DOI:10.1128/jb.159.2.511-519.1984
PMID:6746571
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC215674/
Abstract

Two phenotypically autolysis-deficient strains of Streptococcus faecium ATCC 9790 were shown to produce high-molecular-weight, soluble, linear, uncross-linked peptidoglycan when incubated with benzylpenicillin in a wall medium which permits cell wall synthesis (wall thickening) but not balanced growth. This high-molecular-weight s-peptidoglycan was shown to have a molecular weight of 46,000 to 54,000, lack peptide cross-links, and be virtually devoid of accessory wall polymers. It was hydrolyzed by hen egg white lysozyme and the endogenous, autolytic N-acetylmuramidase of S. faecium, but was not attacked by proteinases. Chemical analyses of the polymer are consistent with the following structure, where n is the number of repeating disaccharide units: (formula; see text).

摘要

已表明,粪肠球菌ATCC 9790的两株表型自溶缺陷菌株,在允许细胞壁合成(细胞壁增厚)但不允许平衡生长的壁培养基中与苄青霉素一起孵育时,会产生高分子量、可溶、线性、未交联的肽聚糖。这种高分子量的s-肽聚糖的分子量为46,000至54,000,缺乏肽交联,并且几乎不含辅助壁聚合物。它可被鸡蛋清溶菌酶和粪肠球菌的内源性自溶N-乙酰胞壁酸酶水解,但不被蛋白酶攻击。该聚合物的化学分析与以下结构一致,其中n是重复二糖单元的数量:(分子式;见正文)。