Abe T, Watanabe M, Sai T, Asano T, Kiho Y
Microbiol Immunol. 1981;25(11):1129-38. doi: 10.1111/j.1348-0421.1981.tb00121.x.
Cetyltrimethylammonium bromide (CTAB) modified tobacco mosaic virus (TMV) virions so that the intrinsic fluorescence changed, viral infectivity decreased, sensitivity to RNase or UV irradiation increased, and coat protein subunits were released by the addition of Triton X-100. The change in fluorescence emission at 320 nm shifted to 340 nm was observed at 100 micrograms of CTAB per ml. This represents a change in the tryptophan environment inside the virion. At a lower concentration of CTAB, intersubunit contact was weakened, resulting in the release of coat protein subunits and an increase in RNase sensitivity. The release of coat protein took place gradually and two relatively stable intermediates were observed. Increase in UV sensitivity was observed at a lower concentration of CTAB and formation of pyrimidine hydrate was involved in this inactivation. The nature of the minor structural change leading to UV inactivation is discussed.
十六烷基三甲基溴化铵（CTAB）修饰烟草花叶病毒（TMV）病毒粒子，使其固有荧光发生变化，病毒感染力下降，对核糖核酸酶或紫外线照射的敏感性增加，并且通过添加 Triton X - 100 可释放外壳蛋白亚基。每毫升 100 微克 CTAB 时，观察到 320 纳米处的荧光发射变化向 340 纳米处移动。这代表病毒粒子内部色氨酸环境的变化。在较低浓度的 CTAB 下，亚基间的接触被削弱，导致外壳蛋白亚基的释放以及核糖核酸酶敏感性的增加。外壳蛋白的释放是逐渐发生的，并且观察到两个相对稳定的中间体。在较低浓度的 CTAB 下观察到紫外线敏感性增加，嘧啶水合物的形成参与了这种失活过程。讨论了导致紫外线失活的微小结构变化的性质。
