Beckey A D, Wulff J L, Earhart C F
J Virol. 1974 Oct;14(4):886-94. doi: 10.1128/JVI.14.4.886-894.1974.
Proteins that associate with cellular membrane during the first 5 min after infection with bacteriophage T4 were examined. Several procedures, including electrophoretic separations in three sodium dodecyl sulfate polyacrylamide gel systems and inhibition of host protein synthesis by UV irradiation, were employed to distinguish host-specified proteins from those induced by T4. Residual host protein synthesis was found to account for much of the new protein in preparations of the total membrane and for almost all of the newly synthesized protein in the outer membrane. Preliminary evidence indicates that the synthesis of some host membrane proteins is shut off less rapidly than is host synthesis of soluble protein. One host-directed polypeptide of the outer membrane was unique in that its synthesis or incorporation into the membrane was preferentially inhibited by infection. Also, it was found that the detergent Sarkosyl solubilizes all early T4 membrane proteins; this observation provides the basis for a simple procedure for distinguishing phage proteins from host outer membrane proteins.
对感染噬菌体T4后最初5分钟内与细胞膜结合的蛋白质进行了检测。采用了多种方法，包括在三种十二烷基硫酸钠聚丙烯酰胺凝胶系统中进行电泳分离以及通过紫外线照射抑制宿主蛋白质合成，以区分宿主特异性蛋白质和T4诱导的蛋白质。发现残余的宿主蛋白质合成占总膜制剂中大部分新蛋白质以及外膜中几乎所有新合成的蛋白质。初步证据表明，一些宿主膜蛋白的合成关闭速度比宿主可溶性蛋白的合成关闭速度慢。外膜中一种由宿主指导的多肽的独特之处在于，其合成或整合到膜中受到感染的优先抑制。此外，还发现去污剂十二烷基肌氨酸钠可溶解所有早期T4膜蛋白；这一观察结果为区分噬菌体蛋白和宿主外膜蛋白的简单方法提供了基础。
