Schlepper J, Knippers R
Eur J Biochem. 1975 Dec 1;60(1):209-20. doi: 10.1111/j.1432-1033.1975.tb20993.x.
Three protein kinase activities are found in nuclei from three different murine cells (Ehrlich ascites cells, mouse L cells and rat glioma cells). Two of these activities are soluble, one is bound to chromatin. The soluble enzymes are similar, if not identical, to the cytoplasmic protein kinases. The chromatin-bound, adenosine-cyclic-3':5'-monophosphate-independent enzyme is not found in the cytoplasm. This enzyme is composed of one subunit with a molecular weight of 80000-90000. Some biochemical properties of this enzyme are described. A brief description of a nuclear enzyme, which dephosphorylates phosphorylated histones, is also given.
在来自三种不同小鼠细胞（艾氏腹水癌细胞、小鼠L细胞和大鼠胶质瘤细胞）的细胞核中发现了三种蛋白激酶活性。其中两种活性是可溶的，一种与染色质结合。这些可溶酶即使不完全相同，也与细胞质蛋白激酶相似。细胞质中未发现与染色质结合的、不依赖于环磷酸腺苷的酶。这种酶由一个分子量为80000 - 90000的亚基组成。描述了这种酶的一些生化特性。还简要介绍了一种能使磷酸化组蛋白去磷酸化的核酶。
