Harborne N, Allan J
FEBS Lett. 1983 May 2;155(1):88-92. doi: 10.1016/0014-5793(83)80215-4.
The order in which the core histone tails in chicken erythrocyte chromatin are attacked by trypsin has been reinvestigated. Results are presented to demonstrate that in the absence of linker histones H1 and H5 the relative order of core histone degradation by trypsin can be altered by changing the salt environment. In native chromatin, the presence of linker histones H1 and H5 inhibits this salt-dependent transition.
鸡红细胞染色质中核心组蛋白尾巴被胰蛋白酶攻击的顺序已被重新研究。研究结果表明,在没有连接组蛋白H1和H5的情况下,通过改变盐环境可以改变胰蛋白酶对核心组蛋白的降解相对顺序。在天然染色质中,连接组蛋白H1和H5的存在会抑制这种盐依赖性转变。