Stone K R, Cummings D J
J Virol. 1970 Oct;6(4):445-54. doi: 10.1128/JVI.6.4.445-454.1970.
Two species of basic internal proteins were found in osmotic shock supernatant solutions of bacteriophages T4B, T4D, T2H, T2L, and T6. The major species of protein isolated had a molecular weight of approximately 21,000 daltons, whereas the minor protein molecular weight was near 9,500 daltons. The two protein species exhibited unique isoelectric points and amino acid compositions. The 21,000-dalton protein of T2L showed major electrophoretic and compositional differences from the other 21,000-dalton proteins isolated. Similarities between the 21,000-dalton proteins and phage lysozyme are discussed.
在噬菌体T4B、T4D、T2H、T2L和T6的渗透压休克上清液中发现了两种基本的内部蛋白质。分离出的主要蛋白质种类的分子量约为21,000道尔顿，而次要蛋白质的分子量接近9,500道尔顿。这两种蛋白质种类表现出独特的等电点和氨基酸组成。T2L的21,000道尔顿蛋白质与分离出的其他21,000道尔顿蛋白质在电泳和组成上存在主要差异。文中讨论了21,000道尔顿蛋白质与噬菌体溶菌酶之间的相似性。
