通过凝胶过滤法对小牛胸腺组蛋白F2(b)进行的一项研究。
A study of calf thymus histone fraction F2(b) by gel filtration.
作者信息
Edwards P A, Shooter K V
出版信息
Biochem J. 1970 Nov;120(1):61-6. doi: 10.1042/bj1200061.
The gel-filtration behaviour of calf thymus histone fraction F2(b) was studied at three different salt concentrations (0.01m-, 0.10m- and 1.00m-sodium chloride) and two different pH ranges (pH3-4 and pH6.7-7.1). Other histone fractions [F1, F2(a) and F3] were also utilized to assist interpretation of the data. It was found that the Stokes radius of histone fraction F2(b) was not significantly changed when the salt concentration was increased, implying that the aggregation of the individual histone molecules (Edwards & Shooter, 1969) resulted in only relatively minor changes in the hydrodynamic volume. Aggregation would appear to be due to the salting out of hydrophobic regions giving rise, in the aggregate, to a compact core of hydrophobic groups from which protrude the remaining basic parts of the molecule. Repulsion between charged groups on the basic regions of individual histone molecules would give the aggregate approximately spherical symmetry, the diameter of the aggregate approximating to the length of a single histone molecule.
在三种不同盐浓度（0.01m -、0.10m -和1.00m -氯化钠）以及两个不同pH范围（pH3 - 4和pH6.7 - 7.1）下研究了小牛胸腺组蛋白F2(b)组分的凝胶过滤行为。还利用了其他组蛋白组分[F1、F2(a)和F3]来辅助解释数据。结果发现，当盐浓度增加时，组蛋白F2(b)组分的斯托克斯半径没有显著变化，这意味着单个组蛋白分子的聚集（爱德华兹和舒特，1969年）仅导致流体动力学体积发生相对较小的变化。聚集似乎是由于疏水区域的盐析作用，在聚集体中形成了一个紧密的疏水基团核心，分子的其余碱性部分从该核心突出。单个组蛋白分子碱性区域上带电基团之间的排斥作用会使聚集体具有近似球形的对称性，聚集体的直径近似于单个组蛋白分子的长度。
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