Schafer-Nielsen C, Rose C
Biochim Biophys Acta. 1982 Mar 29;696(3):323-31. doi: 10.1016/0167-4781(82)90064-1.
A procedure by which chromatin proteins (histones and non-histones) can be rapidly separated from nucleic acids by hydrophobic interaction chromatography is described. The procedure is carried out under non-rigorous conditions that must be assumed to induce little irreversible change in the biological properties of most proteins. More than 90% (w/w) of the chromatin proteins can be retained by hydrophobic interaction while nucleic acids pass quantitatively through the columns. By gradient elution of the columns the histones can be divided into fractions containing H1, H2A/H2B and H3/H4, and at the same time a subfractionation of the non-histone proteins is obtained. Protein recovery depends on the type of column used, but exceeds 80% (w/w) with even the most strongly binding hydrophobic matrix investigated.
本文描述了一种通过疏水相互作用色谱法将染色质蛋白（组蛋白和非组蛋白）与核酸快速分离的方法。该方法在非严格条件下进行，必须假定这种条件对大多数蛋白质的生物学特性几乎不会引起不可逆的变化。超过90%（w/w）的染色质蛋白可通过疏水相互作用保留，而核酸则定量通过柱子。通过对柱子进行梯度洗脱，组蛋白可被分为含有H1、H2A/H2B和H3/H4的组分，同时还可对非组蛋白进行亚分级分离。蛋白质回收率取决于所用柱子的类型，但即使是所研究的结合力最强的疏水基质，回收率也超过80%（w/w）。
