Butler A P, Harrington R E, Olins D E
Nucleic Acids Res. 1979 Apr;6(4):1509-20. doi: 10.1093/nar/6.4.1509.
The inner histone complex, extracted from chicken erythrocyte chromatin in 2 M NaCL AT pH 7.4, has been characterized by sedimentation equilibrium and sedimentation velocity. High speed sedimentation equilibrium studies indicate that in 2 M NaCl the inner histones are a weakly associating system with contributions from species ranging in molecular weight from dimer to octamer. The appearance of a single boundary (3.8S at 2 M NaCl) in sedimentation velocity studies conducted over a wide range of protein concentrations and ionic conditions indicates that the various histone oligomers present are in rapid equilibrium with one another. At higher salts the equilibrium is shifted to favor higher molecular weight species; in 4 M NaCl essentially all of the histone is octameric at protein concentrations above 0.2 mg/ml. The facile interconversion of histone oligomers suggests that small alterations in histone-histone interactions may be responsible for changes in nucleosome conformations during various biological processes.
从处于pH 7.4的2M氯化钠溶液中的鸡红细胞染色质中提取的内部组蛋白复合物，已通过沉降平衡和沉降速度进行了表征。高速沉降平衡研究表明，在2M氯化钠中，内部组蛋白是一个弱缔合系统，其中有分子量从二聚体到八聚体不等的物种的贡献。在广泛的蛋白质浓度和离子条件下进行的沉降速度研究中出现的单一边界（在2M氯化钠中为3.8S）表明，存在的各种组蛋白寡聚体彼此处于快速平衡状态。在较高盐浓度下，平衡向有利于更高分子量物种的方向移动；在4M氯化钠中，当蛋白质浓度高于0.2mg/ml时，基本上所有组蛋白都是八聚体。组蛋白寡聚体的容易相互转化表明，组蛋白-组蛋白相互作用的微小变化可能是各种生物过程中核小体构象变化的原因。
