Hawiger J
J Bacteriol. 1968 Feb;95(2):376-84. doi: 10.1128/jb.95.2.376-384.1968.
A method based on cold ethyl alcohol fractionation at different pH levels and ionic strengths and on gel filtration on a Sephadex G-200 column was used to concentrate and purify lysozyme from the culture supernatant fluid of Staphylococcus aureus strain 524. The final, nondialyzable product exhibited a 163-fold rise in specific activity over that of the starting material. Staphylococcal lysozyme is a glycosidase which splits N-acetylamino sugars from the susceptible substrate. Staphylococcal lysozyme was shown to be similar to egg white lysozyme in its optimal temperature for reaction, optimal pH, activation by NaCl and Ca(++) ions, inhibition by sodium citrate and ethylenediaminetetraacetate, and inactivation by Cu(++) ions and sodium dodecyl sulfate. It differs from the egg white lysozyme in its temperature susceptibility range (staphylococcal lysozyme is inactivated at 56 C). It acts on whole cells and cell walls of Micrococcus lysodeikticus, murein from S. aureus 524, and cell walls of S. epidermidis Zak. The last substrate was not susceptible to the action of egg white lysozyme in the test system used. The mechanism of action of staphylococcal lysozyme seems to be analogous to that of egg white lysozyme; however, the biological specificity of the two enzymes may be different.
采用一种基于在不同pH值和离子强度下进行冷乙醇分级分离以及在葡聚糖凝胶G - 200柱上进行凝胶过滤的方法，从金黄色葡萄球菌524菌株的培养上清液中浓缩和纯化溶菌酶。最终的不可透析产物的比活性比起始原料提高了163倍。葡萄球菌溶菌酶是一种糖苷酶，可从易感底物中裂解N - 乙酰氨基糖。结果表明，葡萄球菌溶菌酶在反应的最佳温度、最佳pH值、被NaCl和Ca(++)离子激活、被柠檬酸钠和乙二胺四乙酸抑制以及被Cu(++)离子和十二烷基硫酸钠灭活等方面与蛋清溶菌酶相似。它在温度敏感性范围方面与蛋清溶菌酶不同（葡萄球菌溶菌酶在56℃时失活）。它作用于溶壁微球菌的全细胞和细胞壁、金黄色葡萄球菌524的胞壁质以及表皮葡萄球菌Zak的细胞壁。在所用的测试系统中，最后一种底物对蛋清溶菌酶的作用不敏感。葡萄球菌溶菌酶的作用机制似乎与蛋清溶菌酶类似；然而，这两种酶的生物学特异性可能不同。
