The lambda head-tail joining reaction: purification, properties and structure of biologically active heads and tails.
The lambda head-tail joining reaction: purification, properties and structure of biologically active heads and tails.
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拉姆达头尾连接反应：生物活性头尾的纯化、性质和结构。
DOI：
10.1016/0022-2836(73)90397-5
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发表时间：
1973
影响因子：
5.6
通讯作者：
V. C. Bode
中科院分区：
文献类型：
--
作者：
D. Harrison;D. T. Brown;V. C. Bode
开发了获得高纯度生物活性λ头部和尾部的方法，回收率为20 - 40%。游离头、游离尾和噬菌体颗粒在稳定性上明显不同。噬菌体在含有Mg 2+的溶液中是稳定的，但尾部不稳定。形成尾轴的蛋白质亚基在Mg 2+存在下解离并形成多亚基球形结构。EDTA保护游离尾部免于失活，但破坏头部和噬菌体颗粒。四碳二胺，腐胺，稳定头部对失活;三碳和五碳二胺是有效性较低。电子显微镜照片揭示了一个新的“旋钮”结构的末端尾纤维的噬菌体和自由的尾巴。从EDTA破坏的噬菌体释放的尾部具有“头-尾连接器”，这是在尾部与头部连接之前不存在的结构。
Procedures were developed to obtain biologically active lambda heads and tails at high purity with 20 to 40% recovery. Free heads, free tails and phage particles differ markedly in stability. Phage are stable in solutions containing Mg2+but tails are not. The protein subunits which form the shaft of the tail dissociate in the presence of Mg2+and form multisubunit spherical structures. EDTA protects free tails against inactivation but disrupts heads and phage particles. The four carbon diamine, putrescine, stabilizes heads against inactivation; the three and five carbon diamines are less effective. Electron micrographs reveal a new “knob” structure at the distal end of the tail fiber of phage and of free tails. Tails released from EDTA-disrupted phage possess a “head-tail connector”, a structure not present on the tail before its joining with a head.