Díaz-Nido J, Avila J
Centro de Biología Molecular (CSIC-UAM), Universidad Autónoma, Madrid, Spain.
Second Messengers Phosphoproteins. 1992;14(1-2):39-53.
Mitotic spindles isolated from prometaphase-arrested mammalian cells contain associated protein kinases that are extracted by high salt treatment. Their fractionation by ion-exchange chromatography reveals three major peaks of protein kinase activity that phosphorylate brain microtubule-associated proteins and differ in their substrate specificity. One of them has been identified as a casein kinaseII-like enzyme. A mitotic spindle-associated 325 kDa protein related to brain MAP1B is a major substrate for this casein kinase II-like enzyme. Another mitotic spindle protein kinase has been tentatively identified as a proline-directed protein kinase.
从处于前中期停滞的哺乳动物细胞中分离出的有丝分裂纺锤体含有相关蛋白激酶,这些激酶可通过高盐处理提取出来。通过离子交换色谱对它们进行分级分离,可揭示出三个主要的蛋白激酶活性峰,这些活性峰可使脑微管相关蛋白磷酸化,且底物特异性不同。其中一个已被鉴定为酪蛋白激酶II样酶。一种与脑MAP1B相关的有丝分裂纺锤体相关325 kDa蛋白是这种酪蛋白激酶II样酶的主要底物。另一种有丝分裂纺锤体蛋白激酶已被初步鉴定为脯氨酸定向蛋白激酶。