Weinbaum G, Rich R, Fischman D A
J Bacteriol. 1967 May;93(5):1693-8. doi: 10.1128/jb.93.5.1693-1698.1967.
Normal and filamentous whole cells and isolated envelopes of Escherichia coli B were exposed to various enzymatic treatments to remove surface layers and to characterize the component(s) conferring rigidity in this organism. Modification of cell rigidity was determined by sphere formation in both whole cells and isolated envelopes. Enzymes capable of converting trypsinized normal or untreated filamentous whole cells and untreated envelopes to spheres included: lysozyme plus ethylenediaminetetraacetic acid, clostridial phospholipase C, and phospholipase D from cabbage. These data suggest that there are at least two components essential for maintenance of cell rigidity in E. coli B. The first is the peptidoglycan (mucopeptide), which is susceptible to lysozyme. The second is a phospholipid which is either covalently linked to the mucopeptide or in close association with it. This phospholipase C-sensitive component is protected more completely in normal than in filamentous whole cells by a protein layer which is easily modified by trypsin treatment to allow enzymatically induced sphere formation to occur.
将大肠杆菌B的正常和丝状全细胞以及分离的包膜进行各种酶处理，以去除表面层并表征赋予该生物体刚性的成分。通过全细胞和分离包膜中的球体形成来确定细胞刚性的改变。能够将胰蛋白酶处理过的正常或未处理的丝状全细胞以及未处理的包膜转化为球体的酶包括：溶菌酶加乙二胺四乙酸、梭菌磷脂酶C和来自卷心菜的磷脂酶D。这些数据表明，在大肠杆菌B中维持细胞刚性至少有两个必需成分。第一个是肽聚糖（粘肽），它对溶菌酶敏感。第二个是一种磷脂，它要么与粘肽共价连接，要么与其紧密结合。这种对磷脂酶C敏感的成分在正常全细胞中比在丝状全细胞中受到蛋白质层更完全的保护，该蛋白质层很容易被胰蛋白酶处理修饰，从而使酶诱导的球体形成得以发生。
