Klump H, Beaumais J, Devauchelle G
Arch Virol. 1983;75(4):269-76. doi: 10.1007/BF01314892.
Structural features and thermodynamic parameters of the complete Chilo iridescent virus (Iridovirus type 6) and its constituents, isolated from the larvae of Galleria mellonella, were evaluated by means of UV spectroscopy and microcalorimetry. It can be demonstrated that the viral DNA is attached to the coat protein in a chromatin-like fashion, which is preserved after disruption of the virus by low temperature or partial digestion of the coat protein with proteinase K. At elevated temperature however the viral DNA is denaturated irreversibly. The coat protein appears to remain in its native state during the DNA transition and its own thermal denaturation profile shows its independence from the DNA denaturation.
通过紫外光谱法和微量量热法对从大蜡螟幼虫中分离出的完整的稻纵卷叶螟虹彩病毒（虹彩病毒6型）及其成分的结构特征和热力学参数进行了评估。可以证明，病毒DNA以染色质样方式附着在衣壳蛋白上，在病毒通过低温破坏或用蛋白酶K对衣壳蛋白进行部分消化后，这种方式仍然保留。然而，在高温下，病毒DNA会不可逆地变性。衣壳蛋白在DNA转变过程中似乎保持其天然状态，其自身的热变性曲线显示出它与DNA变性无关。
