Mathews C K, Crosby L K, Kozloff L M
J Virol. 1973 Jul;12(1):74-8. doi: 10.1128/JVI.12.1.74-78.1973.
Antiserum was prepared against highly purified T4D bacteriophage-induced dihydrofolate reductase (DFR). This serum not only inactivated the enzyme but also inactivated all strains of T4D examined. T6 was inactivated to a lesser extent, and T2L, T2H, and T5 were unaffected by the antiserum. The phage-killing power of the serum could be blocked by prior incubation with partially purified T4D dfr obtained from host cells unable to make phage structural proteins. These observations confirm earlier results that the phage dfr is a structural component of the phage particle, and they offer new evidence on the manner in which this enzyme in incorporated into the tail structure.
制备了针对高度纯化的T4D噬菌体诱导的二氢叶酸还原酶（DFR）的抗血清。该血清不仅使该酶失活，还使所有检测的T4D菌株失活。T6的失活程度较小，而T2L、T2H和T5不受该抗血清的影响。血清的噬菌体杀伤能力可通过与从无法产生噬菌体结构蛋白的宿主细胞中获得的部分纯化的T4D dfr预先孵育来阻断。这些观察结果证实了早期的结果，即噬菌体dfr是噬菌体颗粒的结构成分，并且它们为该酶掺入尾部结构的方式提供了新的证据。
