Sahyoun N, LeVine H, Cuatrecasas P
Proc Natl Acad Sci U S A. 1984 Jul;81(14):4311-5. doi: 10.1073/pnas.81.14.4311.
A major Ca2+/calmodulin-dependent protein kinase has been isolated in association with the neuronal nuclear matrix. Nuclear matrix preparations contain highly phosphorylated polypeptides with Mr values of 50,000 and 60,000. These polypeptides were further characterized by peptide and phospho peptide mapping, two-dimensional isoelectrofocusing/NaDodSO4/PAGE, and 125I-labeled calmodulin binding. The results indicate that the Mr 50,000 and 60,000 polypeptides of the nuclear matrix closely resemble the alpha and beta subunits, respectively, of the Ca2+/calmodulin-dependent protein kinase of the post-synaptic density. These findings indicate that similar protein kinases mediate the neuronal effects of Ca2+ at the cytosolic, synaptosomal, and nuclear levels.
一种主要的钙/钙调蛋白依赖性蛋白激酶已与神经元核基质相关联被分离出来。核基质制剂含有分子量分别为50,000和60,000的高度磷酸化多肽。通过肽和磷酸肽图谱分析、二维等电聚焦/十二烷基硫酸钠/聚丙烯酰胺凝胶电泳以及125I标记的钙调蛋白结合对这些多肽进行了进一步表征。结果表明,核基质的分子量为50,000和60,000的多肽分别与突触后致密部的钙/钙调蛋白依赖性蛋白激酶的α和β亚基非常相似。这些发现表明,类似的蛋白激酶在细胞质、突触体和核水平介导钙对神经元的作用。