Okabayaski K, Mizuno D
J Bacteriol. 1974 Jan;117(1):215-21. doi: 10.1128/jb.117.1.215-221.1974.
The cellular localization of staphylococcus nuclease, previously known as an exoenzyme, was investigated, and the following results were obtained. (i) When Staphylococcus aureus cells were converted to protoplasts by cell wall lytic enzyme L-11 (a bacteriolytic enzyme purified from Flavobacterium sp. which specifically hydrolyzes amide and peptide linkages of murein layers), over 80% of the cell-bound nuclease was released into the surrounding sucrose medium. (ii) The cell-bound nuclease was associated with the cell-wall membrane fraction of mechanically disrupted cells. (iii) The nuclease activity of cell-wall membrane fractions from cells during early and late stages of protoplast formation were compared. Less activity was found in the late stage. These results suggest that nuclease may be located at or near the surface of the cells. The distribution of cell-bound nuclease in the cell-wall membrane fraction varied with the growth conditions of S. aureus. The activity of alkaline phosphatase, another surface enzyme, was also investigated. Less of this enzyme than nuclease was released when the cells were converted to protoplasts.
对以前被认为是一种胞外酶的葡萄球菌核酸酶的细胞定位进行了研究,获得了以下结果。(i) 当金黄色葡萄球菌细胞被细胞壁裂解酶L-11(一种从黄杆菌属中纯化的溶菌酶,它特异性水解胞壁质层的酰胺和肽键)转化为原生质体时,超过80%的细胞结合核酸酶被释放到周围的蔗糖培养基中。(ii) 细胞结合核酸酶与机械破碎细胞的细胞壁膜部分相关。(iii) 比较了原生质体形成早期和晚期细胞的细胞壁膜部分的核酸酶活性。在晚期发现的活性较低。这些结果表明核酸酶可能位于细胞表面或其附近。细胞结合核酸酶在细胞壁膜部分的分布随金黄色葡萄球菌的生长条件而变化。还研究了另一种表面酶碱性磷酸酶的活性。当细胞转化为原生质体时,这种酶比核酸酶释放得少。