Nugent K M, Huff E, Cole R M, Theodore T S
J Bacteriol. 1974 Dec;120(3):1012-6. doi: 10.1128/jb.120.3.1012-1016.1974.
Staphylococus aureus, ATCC 6538P, was fractionated into protoplast membranes, mesosomal vesicles, periplasm, and cytoplasm. These fractions and the culture fluid were then assayed for various degradative enzyme activities. They were not restricted to a single fraction nor dispersed homogeneously, but were distributed predominantly (on the basis of specific activity) as follows: nuclease in the culture fluid; alkaline phosphatase, 5'-nucleotidase, and acid phosphatase in the periplasm; adenosine triphosphatase in the protoplast membrane; and protease (low levels) in mesosomal vesicles. No significant esterase nor cell wall hydrolytic activity was found in any fraction. S. aureus 80/81 was studied for penicillinase activity after induction with benzyl penicillin; this enzyme was localized in the mesosomal vesicles. Electron microscopy did not reveal any ultrastructural changes associated with secretion of the extracellular fraction. Overall, these studies demonstrate that degradative enzymes are located in several surface compartments and that, therefore, the mesosome does not function as a prototype lysosome in S. aureus.
将金黄色葡萄球菌ATCC 6538P分离成原生质体膜、间体囊泡、周质和细胞质。然后对这些组分以及培养液进行各种降解酶活性检测。这些酶并非局限于单一组分,也不是均匀分布,而是主要(基于比活性)分布如下:培养液中的核酸酶;周质中的碱性磷酸酶、5'-核苷酸酶和酸性磷酸酶;原生质体膜中的三磷酸腺苷酶;间体囊泡中的蛋白酶(含量低)。在任何组分中均未发现明显的酯酶和细胞壁水解活性。在用苄青霉素诱导后,对金黄色葡萄球菌80/81的青霉素酶活性进行了研究;该酶定位于间体囊泡中。电子显微镜未发现与细胞外组分分泌相关的任何超微结构变化。总体而言,这些研究表明降解酶位于几个表面区室,因此,间体在金黄色葡萄球菌中并不作为典型的溶酶体发挥作用。