Davie J R, Candido E P
Proc Natl Acad Sci U S A. 1978 Aug;75(8):3574-7. doi: 10.1073/pnas.75.8.3574.
Chromatin from trout testis at an early stage of development was digested with DNase II (deoxyribonucleate 3'-oligonucleotidohydrolase; EC 3.1.4.6), and the solubilized products were fractionated into Mg2+-soluble and -insoluble components. An examination of the histones from these fractions by one- and two-dimensional polyacrylamide gels showed that the highly acetylated species of histone H4 (di-, tri-, and tetra-acetylated) were associated mainly with the Mg2+-soluble material. Digestion of this chromatin fraction with pancreatic ribonuclease converted more than half of it to an insoluble state, and the acetylated H4 remained associated with the precipitated fraction. No changes in the other histones were noted, but two other basic proteins were also found to be associated with the Mg2+-soluble fraction. Since this fraction is enriched in transcribing gene sequences, it is concluded that the histone H4 of active genes is present in a highly acetylated state.
处于发育早期的鳟鱼睾丸染色质用脱氧核糖核酸酶II（脱氧核糖核酸3'-寡核苷酸水解酶；EC 3.1.4.6）进行消化，然后将溶解产物分离为Mg2+可溶性和不可溶性成分。通过一维和二维聚丙烯酰胺凝胶对这些组分中的组蛋白进行检测，结果显示，高度乙酰化的组蛋白H4（二乙酰化、三乙酰化和四乙酰化）主要与Mg2+可溶性物质相关。用胰核糖核酸酶消化该染色质组分后，超过一半的组分转变为不溶状态，而乙酰化的H4仍与沉淀组分相关。未观察到其他组蛋白有变化，但还发现另外两种碱性蛋白也与Mg2+可溶性组分相关。由于该组分富含正在转录的基因序列，因此得出结论，活性基因的组蛋白H4以高度乙酰化状态存在。
