Parker V H, Stevens C
Chem Biol Interact. 1979 Jul;26(2):167-77. doi: 10.1016/0009-2797(79)90020-6.
In vitro beryllium (Be) binding to rat liver nuclei has been reassessed (KAss = 2.0 X 10(6) M: n = 17 nmol Be/mg protein). Be also binds to rat liver nucleoli (KAss approx. 4 X 10(6) M: n = 10 nmol Be/mg protein). Examination of rat liver chromatin fractionated on a hydroxyapatite column shows that Be does not bind to histone or to the non-histone protein eluted by 0.05 M sodium phosphate. Be is strongly bound to the non-histone proteins eluted by 0.2 M sodium phosphate (KAss = 1.1 X 10(6) M: n = 55 nmol Be/mg protein) and also to the same extent to the fraction containing DNA which is subsequently eluted from the column. Evidence is provided that the latter binding is not due to DNA. The fractions containing the Be-binding proteins also contain the proteins which are phosphorylated to the greater extent.
已重新评估体外铍（Be）与大鼠肝细胞核的结合情况（结合常数KAss = 2.0×10⁶ M：n = 17 nmol Be/mg蛋白质）。铍也与大鼠肝核仁结合（结合常数KAss约为4×10⁶ M：n = 10 nmol Be/mg蛋白质）。对在羟基磷灰石柱上分级分离的大鼠肝染色质进行检测表明，铍不与组蛋白或被0.05 M磷酸钠洗脱的非组蛋白结合。铍与被0.2 M磷酸钠洗脱的非组蛋白紧密结合（结合常数KAss = 1.1×10⁶ M：n = 55 nmol Be/mg蛋白质），并且与随后从柱上洗脱的含DNA部分的结合程度相同。有证据表明，后者的结合并非由DNA引起。含有铍结合蛋白的部分也含有磷酸化程度更高的蛋白质。
