Szewczyk B, Skórko R
Biochim Biophys Acta. 1981 Nov 13;662(1):131-7. doi: 10.1016/0005-2744(81)90233-3.
Bacteriophage T4 ghosts were found to possess lysozyme (mucopeptide N-acetylmuramoylhydrolase, EC 3.2.1.17) activity. This enzyme is probably responsible for the lysis from without, observed at high multiplicity of infection, a process independent of the presence of the e gene product which is also a lysozyme. The ghost lysozyme and e lysozyme differed with respect to their requirements for maximal catalytic activity and to some extent in substrate specificity. The ghost lysozyme was released from phage particle by the action of Triton X-100.
发现噬菌体T4空壳具有溶菌酶（粘肽N - 乙酰胞壁酰水解酶，EC 3.2.1.17）活性。这种酶可能是在高感染复数时观察到的从外部裂解的原因，这一过程独立于同样是溶菌酶的e基因产物的存在。空壳溶菌酶和e溶菌酶在最大催化活性的需求方面以及在某种程度上在底物特异性方面有所不同。空壳溶菌酶通过Triton X - 100的作用从噬菌体颗粒中释放出来。
