Huff E, Silverman C S
J Bacteriol. 1968 Jan;95(1):99-106. doi: 10.1128/jb.95.1.99-106.1968.
Enzyme preparations of Staphylococcus aureus were examined for their ability to solubilize (32)P-labeled cell walls of the parent organism. Enzymatic activity was observed in the growth medium, in soluble fractions, and associated with native cell walls. Enzyme associated with isolated cell walls could be inactivated with formaldehyde without reducing the susceptibility of the walls to the action of added enzyme. When cells are frozen and thawed, 50 to 75% of the intracellular enzyme is released along with 2% of the intracellular protein. This freeze-thaw extracted enzyme has little, if any, activity on intact S. aureus cells. It appears that the enzyme resides near the cell wall and acts on the cell-wall inner surface.
对金黄色葡萄球菌的酶制剂进行了检测，以考察其溶解亲本生物体的（32）P标记细胞壁的能力。在生长培养基、可溶性组分中观察到了酶活性，并且酶活性与天然细胞壁相关。与分离的细胞壁相关的酶可用甲醛使其失活，而不会降低细胞壁对添加酶作用的敏感性。当细胞冻融时，50%至75%的细胞内酶与2%的细胞内蛋白质一起释放出来。这种冻融提取的酶对完整的金黄色葡萄球菌细胞几乎没有活性（如果有活性的话）。看来该酶位于细胞壁附近，并作用于细胞壁的内表面。
