Szewczyk B, Skórko R
Eur J Biochem. 1983 Jul 1;133(3):717-22. doi: 10.1111/j.1432-1033.1983.tb07521.x.
Bacteriophage T4 particle-associated lysozyme, purified to electrophoretic homogeneity, was found to be a protein with a relative molecular mass of 15000. The lysozyme was purified from the particles of bacteriophage T4 e mutant and from the lysates of the 5tsl e T4 mutant, in which the enzyme is in soluble form. In the purification procedure advantage was taken of the affinity of the enzyme for GlcNAc-MurNac-LAla-DGlu-msA2pm-DAla (C6 muropeptide), one of the products of the digestion of Escherichia coli murein with lysozyme. The test for the quick estimation of bacteriolytic activity of the enzyme, using E. coli B freeze-dried cells, is described. The pH optimum of the particle-associated lysozyme was equal to about 6.0, ionic strength optimum to 0.05-0.1 M, and optimum Triton X-100 concentration to 1%, when this substrate was used. Some of the aspects of the possible biological significance of the particle-associated lysozyme in bacteriophage T4 infection are discussed.
纯化至电泳纯的噬菌体T4颗粒相关溶菌酶是一种相对分子质量为15000的蛋白质。该溶菌酶从噬菌体T4 e突变体颗粒以及5tsl e T4突变体的裂解物中纯化得到，在后者中该酶呈可溶形式。在纯化过程中，利用了该酶对GlcNAc-MurNac-LAla-DGlu-msA2pm-DAla（C6 胞壁肽）的亲和力，它是溶菌酶消化大肠杆菌胞壁质的产物之一。描述了使用大肠杆菌B冻干细胞快速评估该酶溶菌活性的试验。当使用此底物时，颗粒相关溶菌酶的最适pH约为6.0，最适离子强度为0.05 - 0.1 M，最适Triton X - 100浓度为1%。讨论了噬菌体T4感染中颗粒相关溶菌酶可能的生物学意义的一些方面。
