Boulikas T
Anal Biochem. 1985 Sep;149(2):379-86. doi: 10.1016/0003-2697(85)90586-x.
The electrophoretic mobilities of calf thymus histones and high-mobility-group (HMG) nonhistone proteins were studied on a newly modified polyacrylamide gel containing acetic acid, urea, and the nonionic detergent Triton X-100 in combination with glycine in the electrode buffer. This gel system avoids stacking gel, photopolymerization of acrylamide, and preelectrophoresis. Under extremely low Triton concentrations some H3 variant forms (H3.1) were preferentially separated by their slower migration from bulk H3. Under increasing concentrations of Triton in the gel in the presence of 3 or 6 M urea, the mobilities of H2A.1, H3.2, H2A.2, H4, and H2B were sequentially retarded. The mobilities of H1 and HMGs remained virtually unchanged under all conditions. This gel system is able to resolve charge-modified histones.
在一种新改良的聚丙烯酰胺凝胶上研究了小牛胸腺组蛋白和高迁移率族（HMG）非组蛋白的电泳迁移率，该凝胶含有乙酸、尿素、非离子去污剂 Triton X - 100，并在电极缓冲液中与甘氨酸结合使用。这种凝胶系统避免了堆积凝胶、丙烯酰胺的光聚合反应和预电泳。在极低的 Triton 浓度下，一些 H3 变体形式（H3.1）因其迁移速度比整体 H3 慢而被优先分离。在凝胶中 Triton 浓度增加且存在 3 或 6 M 尿素的情况下，H2A.1、H3.2、H2A.2、H4 和 H2B 的迁移率依次减慢。在所有条件下，H1 和 HMGs 的迁移率几乎保持不变。这种凝胶系统能够分辨电荷修饰的组蛋白。
