Sonstein S A, Hammel J M, Bondi A
J Bacteriol. 1971 Aug;107(2):499-504. doi: 10.1128/jb.107.2.499-504.1971.
A lytic enzyme active against viable, intact staphylococci is released into culture fluids upon lysis of bacteriophage-infected Staphylococcus aureus PS53 cells. This enzyme, staphylococcal phage-associated lysin (PAL), was partially purified by ammonium sulfate precipitation and gel filtration through Sephadex G-200. PAL is optimally active at pH 6.5 and 30 C, and lytic activity is greatly enhanced by the addition of reducing agents. Lytic activity was observed against all strains of staphylococci tested and against purified staphylococcal cell walls, but no activity was noted against other bacterial species. PAL possesses peptidase activity and results in the production of spheroplasts which can be osmotically stabilized for extended periods by the addition of 7.5% polyethylene glycol 4000.
一种对活的、完整的葡萄球菌有活性的裂解酶，在噬菌体感染的金黄色葡萄球菌PS53细胞裂解时释放到培养液中。这种酶，即葡萄球菌噬菌体相关溶素（PAL），通过硫酸铵沉淀和经Sephadex G - 200凝胶过滤进行了部分纯化。PAL在pH 6.5和30℃时活性最佳，添加还原剂可大大增强其裂解活性。观察到对所有测试的葡萄球菌菌株以及纯化的葡萄球菌细胞壁都有裂解活性，但对其他细菌种类没有活性。PAL具有肽酶活性，会导致原生质球的产生，通过添加7.5%的聚乙二醇4000可使其在较长时间内实现渗透稳定。
