Rao M R, Rao B J, Ganguly J
Biochem J. 1982 Jul 1;205(1):15-21. doi: 10.1042/bj2050015.
Nucleosome core particles and oligonucleosomes were isolated by digesting rat testis nuclei with micrococcal nuclease to 20% acid-solubility, followed by fractionation of the digest on a Bio-Gel A-5m column. The core particles thus isolated were characterized on the basis of their DNA length of 151 +/- 5 base-pairs and sedimentation coefficient of 11.4S. Analysis of the acid-soluble proteins of the core particles indicated that histones TH2B and X2 are constituents of the core particles, in addition to the somatic histones H2A, H2B, H3 and H4. The acid-soluble proteins of the oligonucleosomes comprised all the histones, including both the somatic (H1, H2A, H2B, H3, H4 and X2) and the testis-specific ones (TH1 and TH2B). It was also observed that histones TH1 and H1 are absent from the core particles and were readily extracted from the chromatin by 0.6 M-NaCl, which indicated that both of them are bound to the linker DNA.
通过用微球菌核酸酶将大鼠睾丸细胞核消化至20%酸溶性，随后在Bio-Gel A-5m柱上对消化产物进行分级分离，从而分离出核小体核心颗粒和寡核小体。如此分离出的核心颗粒根据其151±5个碱基对的DNA长度和11.4S的沉降系数进行表征。对核心颗粒的酸溶性蛋白质分析表明，除了体细胞组蛋白H2A、H2B、H3和H4外，组蛋白TH2B和X2也是核心颗粒的组成成分。寡核小体的酸溶性蛋白质包含所有组蛋白，包括体细胞组蛋白（H1、H2A、H2B、H3、H4和X2）和睾丸特异性组蛋白（TH1和TH2B）。还观察到核心颗粒中不存在组蛋白TH1和H1，并且它们很容易被0.6M NaCl从染色质中提取出来，这表明它们都与连接DNA结合。
