通过亲和色谱法对组蛋白-组蛋白相互作用的研究。

A study of histone-histone interactions by affinity chromatography.

作者信息

Jasinskas A L, Gineitis A A

出版信息

Mol Biol Rep. 1976 Sep;3(1):19-25. doi: 10.1007/BF00357205.

Abstract

Homologous whole histone from calf thymus was adsorbed on Sepharose 4B columns with covalently coupled histone fractions H2a, H2b, H3 or H4 in 0.01 M phosphate buffer, pH 6.7 - 1 M NaCl. The adsorbed histones were eluted from the columns with 5 M urea in the same buffer. Electrophoretic analysis has shown that the different columns exhibit selective affinity to the histone fractions: the H2b column to histone H2b and H2a (with only weak affinity to histones H3 and H4), the H2a column to histones H2b and H3 (moderate affinity to histone H2b), and the H4 column to histone H3, H4 and H2b (weak affinity to histone H2a). Histone H1 displayed no fixation by either of the columns tested.

摘要

来自小牛胸腺的同源全组蛋白在pH 6.7的0.01 M磷酸盐缓冲液 - 1 M氯化钠中被吸附到共价偶联有组蛋白组分H2a、H2b、H3或H4的琼脂糖4B柱上。吸附的组蛋白在相同缓冲液中用5 M尿素从柱上洗脱。电泳分析表明，不同的柱对组蛋白组分表现出选择性亲和力：H2b柱对组蛋白H2b和H2a（对组蛋白H3和H4只有弱亲和力），H2a柱对组蛋白H2b和H3（对组蛋白H2b有中等亲和力），H4柱对组蛋白H3、H4和H2b（对组蛋白H2a有弱亲和力）。组蛋白H1在所测试的任何柱上均未显示固定作用。