Bustin M, Simpson R T, Sperling R, Goldblatt D
Biochemistry. 1977 Nov 29;16(24):5281-5. doi: 10.1021/bi00643a033.
Interaction of affinity chromatographically purified antihistone H3 and antihistone H4 with isolated HeLa core particles, followed by separation of unreacted and reacted particles by sedimentation, demonstrates that every core particle contains these histones. Taken together with our previous data indicating the presence of H2B in every nucleosome (Simpson, R. T., and Bustin, M. (1976), Biochemistry 15, 4305), these data lead to the conclusion that each core particle contains two each of the four smaller histones. In contrast to the lack of interference in binding of more than one molecule of antibody to a single species of histone to the core particle, steric hindrance exists when attempts are made to bind both anti-H3 and anti-H4 to core particles.
通过亲和层析纯化的抗组蛋白H3和抗组蛋白H4与分离的HeLa核心颗粒相互作用，随后通过沉降分离未反应和已反应的颗粒，结果表明每个核心颗粒都含有这些组蛋白。结合我们之前表明每个核小体中存在H2B的数据（辛普森，R.T.，和巴斯廷，M.（1976年），《生物化学》15卷，4305页），这些数据得出结论：每个核心颗粒包含四种较小组蛋白各两个。与一种组蛋白的多个抗体分子与核心颗粒结合时不存在干扰不同，当试图将抗H3和抗H4都与核心颗粒结合时存在空间位阻。
