Association of tissue-specific histones with deoxyribonucleic acid. Thermal denaturation of native, partially dehistonized, and reconstituted chromatins.
Association of tissue-specific histones with deoxyribonucleic acid. Thermal denaturation of native, partially dehistonized, and reconstituted chromatins.
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组织特异性组蛋白与脱氧核糖核酸的关联。
DOI：
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发表时间：
1975
期刊：
影响因子：
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通讯作者：
Hnilica Ls
中科院分区：
文献类型：
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作者：
Tsai Yh;Ansevin At;Hnilica Ls
：一阶导数热变性配置文件进行了比较，从鸡红细胞，鸡肝，和海胆（球海胆）精子制备的染色质样品。各种组蛋白组分，包括组织特异性F2c和γ组蛋白的选择性解离，表现在热变性概况的特征性变化中。由此得出结论，可以用特定的热变性温度来鉴定单个组蛋白组分与DNA的结合。通过对杂交染色质的变性实验验证了这一观察结果。鸡红细胞染色质缺乏F2c组蛋白，并用分离的肝F1组蛋白重建，其变性类似鸡肝染色质。相反，鸡肝染色质缺乏F1组蛋白和重建与分离的F2C馏分表现出热变性的鸡红细胞染色质的特征。换句话说，重构染色质的热变性谱近似地由贡献组蛋白组分的总和确定。组成不同的核蛋白的衍生热变性配置文件之间的明显区别，表明热变性灵敏地检测组蛋白含量的变化，因此是染色质制剂的常规表征的一个有价值的工具。
: First derivative thermal denaturation profiles were compared for chromatin samples prepared from chicken erythrocytes, chicken liver, and sea urchin (Strongylocentrotus purpuratus) sperm. Selective dissociation of various histone fractions, including tissue-specific F2c and gamma histones, was manifested in characteristic changes of the thermal denaturation profiles. It was concluded that the binding of individual histone fractions to the DNA can be identified with paricular temperatures of thermal denaturation. This observation was tested by denaturation experiments on hybrid chromatins. Chicken erythrocyte chromatin devoid of F2c histone and reconstituted with isolated liver F1 histone denatured like chicken liver chromatin. Conversely, chicken liver chromatin devoid of F1 histones and reconstituted with isolated F2c fraction exhibited a thermal denaturation profile characteristic of the chicken erythrocyte chromatin. In other words, the thermal denaturation profile of reconstituted chromatin was determined approximately by the sum of contribution histone fractions. The obvious distinctions recognized among the derivative thermal denaturation profiles of compositionally different nucleoproteins suggest that thermal denaturation sensitively detects variations in histone content and therefore is a valuable tool for the routine characterization of chromatin preparations.