Department of Botany, University of Georgia, Athens, Georgia 30610.
Plant Physiol. 1978 Sep;62(3):434-7. doi: 10.1104/pp.62.3.434.
A casein-type protein kinase has been isolated from cauliflower (Brassica cauliflora Gars.) nuclei and purified to a specific activity of 23,000 units/milligram of protein (1 unit is defined as the transfer of 1 picomole of (32)Pi from gamma-[(32)P]ATP to substrate per minute at 28 C). The enzyme has a molecular weight of approximately 39,000 as judged by sucrose density gradient sedimentation. The casein kinase requires ATP as the phosphate donor and will phosphorylate casein and phosvitin, but not histones. The enzyme activity is not affected by cAMP or cGMP. The casein kinase appears to be analogous to casein kinases described in other plant and animal systems.
已从花椰菜（ Brassica cauliflora Gars.）核中分离出一种酪蛋白型蛋白激酶，并将其纯化至特定活性 23,000 单位/毫克蛋白质（1 单位定义为在 28°C 下每分钟将 1 皮摩尔（32）Pi 从 γ-[(32)P]ATP 转移到底物）。该酶的分子量约为 39,000，根据蔗糖密度梯度沉降判断。酪蛋白激酶需要 ATP 作为磷酸供体，并可磷酸化酪蛋白和磷酸化卵黄蛋白，但不能磷酸化组蛋白。该酶的活性不受 cAMP 或 cGMP 的影响。这种酪蛋白激酶似乎类似于在其他植物和动物系统中描述的酪蛋白激酶。
