Nelson E T, Buller C S
J Virol. 1974 Sep;14(3):479-84. doi: 10.1128/JVI.14.3.479-484.1974.
Phospholipase activity has been found to be associated with T4 phage and T4 ghost particles. The attachment of the phospholipase to the phage persists during purification through cesium chloride gradients and dialysis, indicating that it is firmly bound. The presence of the enzymatic activity on T4 ghosts suggests that it is not normally packaged within the head of the virus. The enzyme has specificity for phosphatidylglycerol and its activity is stimulated by 0.1% Triton X-100 and 20% methanol. It does not have a requirement for Ca(2+) and is inactivated at temperatures above 60 C. The association of the phospholipase with T4 phage grown in a phospholipase-deficient host and its absence on unsuppressed T4amtA3 suggests that it may be phage gene specific.
已发现磷脂酶活性与T4噬菌体和T4空壳颗粒有关。在通过氯化铯梯度离心和透析进行纯化的过程中,磷脂酶与噬菌体的结合持续存在,这表明它结合牢固。T4空壳颗粒上存在酶活性,这表明它通常不会被包装在病毒头部。该酶对磷脂酰甘油具有特异性,其活性受到0.1% Triton X-100和20%甲醇的刺激。它不需要Ca(2+),并且在温度高于60℃时失活。磷脂酶与在缺乏磷脂酶的宿主中生长的T4噬菌体的关联以及在未抑制的T4amtA3上不存在该酶,表明它可能具有噬菌体基因特异性。