Stros M, Shick V V, Belyavsky A V, Mirzabekov A D
Mol Biol Rep. 1985 Oct;10(4):221-6. doi: 10.1007/BF00775979.
The binding of isolated high mobility group proteins HMG (1 + 2) with nucleosomes was studied using gel electrophoresis. The interaction of HMG (1 + 2) with mononucleosomes could be detected as a new discrete electrophoretic band with a decreased mobility only after cross-linking of HMG (1 + 2)-nucleosome complex by formaldehyde. Approximately two molecules of the large HMG proteins were bound per nucleosomal particle of a DNA length of approximately 185 base pairs, lacking histones H1 and H5. Using the same techniques, no binding was observed with core particles of a DNA length of approximately 145 base pairs.
使用凝胶电泳研究了分离出的高迁移率族蛋白HMG（1 + 2）与核小体的结合。只有在用甲醛交联HMG（1 + 2）-核小体复合物后，HMG（1 + 2）与单核小体的相互作用才能被检测为一条迁移率降低的新离散电泳带。每个DNA长度约为185个碱基对、缺乏组蛋白H1和H5的核小体颗粒大约结合两个大HMG蛋白分子。使用相同技术，未观察到与DNA长度约为145个碱基对的核心颗粒有结合。
