噬菌体phi 6核衣壳的十二面体框架由蛋白质P1组成。
The dodecahedral framework of the bacteriophage phi 6 nucleocapsid is composed of protein P1.
作者信息
Ktistakis N T, Lang D
出版信息
J Virol. 1987 Aug;61(8):2621-3. doi: 10.1128/JVI.61.8.2621-2623.1987.
The outer layer of the bacteriophage phi 6 nucleocapsid (NC) was removed by EDTA and reassociated with the core in the presence of Ca2+ or Mg2+. The core was relatively inaccessible to trypsin digestion, was composed of protein P1, and was in the dodecahedral framework reported previously. (H.T. Steely, Jr., and D. Lang, J. Virol. 51:479-483, 1984; Y. Yang and D. Lang, J. Virol. 51:484-488, 1984). The double-stranded RNA genome became RNase sensitive after EDTA treatment of the nucleocapsid.
通过乙二胺四乙酸（EDTA）去除噬菌体phi 6核衣壳（NC）的外层，并在Ca2+或Mg2+存在的情况下使其与核心重新结合。核心对胰蛋白酶消化相对不敏感，由蛋白质P1组成，并且处于先前报道的十二面体框架中。（小H.T. 斯蒂利和D. 朗，《病毒学杂志》51:479 - 483，1984年；杨Y. 和D. 朗，《病毒学杂志》51:484 - 488，1984年）。用EDTA处理核衣壳后，双链RNA基因组对核糖核酸酶（RNase）变得敏感。
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