Purification of a protein kinase from human Namalwa cells that phosphorylates topoisomerase I.
Purification of a protein kinase from human Namalwa cells that phosphorylates topoisomerase I.
复制标题
从人 Namalwa 细胞中纯化磷酸化拓扑异构酶 I 的蛋白激酶。
DOI：
10.1016/0006-291x(82)91907-6
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发表时间：
1982
影响因子：
3.1
通讯作者：
Durban,E
中科院分区：
文献类型：
--
作者：
Mills,JS;Busch,H;Durban,E
一个核蛋白激酶磷酸化磷蛋白110 8.4，最近被确定为拓扑异构酶I，已被纯化约330倍，从10 mM的人Namalwa细胞的Tris提取物。该激酶经DEAE-Sephacel柱层析后，再经Sepharose柱亲和层析纯化。该蛋白激酶对拓扑异构酶I表现出高亲和力（Km= 0.3 μM）;其对阿托维汀的亲和力约低100倍（Km= 25 μM）。
A nuclear protein kinase which phosphorylates phosphoprotein 110 8.4, recently identified as topoisomerase I, has been purified approximately 330 fold from a 10 mM Tris extract of human Namalwa cells. The kinase wás chromatographed on DEAE-Sephacel and further purified by affinity chromatography on phosvitin-Sepharose. The protein kinase exhibited a high affinity (Km= 0.3 μM) for topoisomerase I; its affinity for phosvitin was approximately 100 fold lower (Km= 25 μM).