Kiho Y, Abe T
Microbiol Immunol. 1980;24(7):617-28. doi: 10.1111/j.1348-0421.1980.tb02864.x.
Combined action of polyornithine and lecithin modified tobacco mosaic virus (TMV) virions making them sensitive to ribonuclease (RNase), pronase or Triton X-100. Sedimentational analysis and examination of the fluorescence spectrum revealed that the reaction product obtained after RNase treatments of modified TMV was a three-component complex made of coat protein, polyornithine and lecithin. The minimum requirement for the modification was completely fulfilled by cetyltrimethylammonium bromide, suggesting that a positively charged nitrogen group and an alkyl group of moderate size, C10--18, are necessary components. These components react with the surface region of TMV which is considered to have an important role in connecting coat protein subunits in TMV virions.
多聚鸟氨酸和卵磷脂共同作用修饰烟草花叶病毒（TMV）病毒粒子，使其对核糖核酸酶（RNase）、链霉蛋白酶或曲拉通X-100敏感。沉降分析和荧光光谱检测表明，经RNase处理的修饰TMV后得到的反应产物是一种由衣壳蛋白、多聚鸟氨酸和卵磷脂组成的三元复合物。十六烷基三甲基溴化铵完全满足了修饰的最低要求，这表明带正电荷的氮基团和中等大小（C10 - 18）的烷基是必需成分。这些成分与TMV的表面区域发生反应，该表面区域被认为在连接TMV病毒粒子中的衣壳蛋白亚基方面具有重要作用。
