Carballo M, Puigdomènech P, Palau J
EMBO J. 1983;2(10):1759-64. doi: 10.1002/j.1460-2075.1983.tb01654.x.
High mobility group (HMG) proteins 1 and 2 from calf thymus have been digested under structuring conditions (0.35 M NaCl, pH 7.1) with two proteases of different specificities, trypsin and V8. The two proteases give a different but restricted pattern of peptides in a time course digestion study. However, when the interactions of the peptides with DNA are studied by blotting, a closely related peptide from HMG-1 and -2 does not show any apparent binding. This peptide, from the V8 protease digestion, has been isolated by DNA-cellulose chromatography and has the amino acid composition predicted for a fragment containing the two C-terminal domains of the protein, i.e., approximately residues 74-243 for HMG-1. The same peptide shows the only interaction detectable with labelled histone H1. A separate function for the different domains of HMG proteins 1 and 2 is proposed.
来自小牛胸腺的高迁移率族（HMG）蛋白1和2在结构化条件（0.35M NaCl，pH 7.1）下用两种具有不同特异性的蛋白酶——胰蛋白酶和V8蛋白酶进行了消化。在时间进程消化研究中，这两种蛋白酶产生了不同但有限的肽段模式。然而，当通过印迹法研究肽段与DNA的相互作用时，来自HMG-1和-2的一个密切相关的肽段并未显示出任何明显的结合。这个来自V8蛋白酶消化的肽段已通过DNA-纤维素色谱法分离出来，其氨基酸组成与预测的包含该蛋白两个C末端结构域的片段相符，即HMG-1约为第74至243位氨基酸残基。相同的肽段显示出与标记的组蛋白H1之间唯一可检测到的相互作用。本文提出了HMG蛋白1和2不同结构域的独立功能。
