Okabayashi K, Mizuno D
J Bacteriol. 1974 Jan;117(1):222-6. doi: 10.1128/jb.117.1.222-226.1974.
The surface-bound nuclease of Staphylococcus aureus liberated during formation of protoplasts was purified 1,000-fold by chromatography on phosphocellulose. Its properties were compared with those of the known extracellular nuclease, purified 200-fold by the same procedures. The adsorbance of the surface-bound nuclease on phosphocellulose was distinctly different from that of the extracellular nuclease, but other properties of the two enzymes were similar. Both enzymes had a pH optimum of about 10 and required Ca(2+) for activity. Both enzymes hydrolyzed deoxyribonucleic acid (DNA) and ribonucleic acid, and denatured DNA was a better substrate than native DNA. Both enzymes were inhibited by the same metal ions. Nuclease-less mutants of S. aureus were isolated from S. aureus 209P by using N-methyl-N'-nitroso-N-nitrosoguanidine. These mutants contained neither surface-bound nor extracellular nuclease activity. These results suggest that the surface-bound and extracellular nucleases are expressed from the same cistron of S. aureus.
在原生质体形成过程中释放的金黄色葡萄球菌表面结合核酸酶，通过磷酸纤维素柱层析纯化了1000倍。将其性质与通过相同程序纯化了200倍的已知细胞外核酸酶的性质进行了比较。表面结合核酸酶在磷酸纤维素上的吸附与细胞外核酸酶明显不同，但两种酶的其他性质相似。两种酶的最适pH约为10，且活性需要Ca(2+)。两种酶都能水解脱氧核糖核酸（DNA）和核糖核酸，变性DNA比天然DNA是更好的底物。两种酶都受到相同金属离子的抑制。通过使用N-甲基-N'-亚硝基-N-亚硝基胍从金黄色葡萄球菌209P中分离出无核酸酶的金黄色葡萄球菌突变体。这些突变体既不具有表面结合核酸酶活性也不具有细胞外核酸酶活性。这些结果表明，表面结合核酸酶和细胞外核酸酶是由金黄色葡萄球菌的同一顺反子表达的。
