Weller M, Morgan I
Biochim Biophys Acta. 1976 Jul 1;436(3):675-85. doi: 10.1016/0005-2736(76)90449-1.
The subcellular distribution of histone and phosvitin kinase activities in brain has been studied and the ability of the various fractions to catalyse the phosphorylation of their endogenous proteins (intrinsic protein kinase activity) also examined. Synaptosome membrane fragments have little or no histone or phosvitin kinase activity but contain the highest concentration of cyclic AMP-stimulated intrinsic protein kinase activity. Homogenisation of the membrane fragments in Triton X-100 increased the histone kinase activity but on centrifugation it was all recovered in the supernatant, while the insoluble material contained all the intrinsic protein kinase activity. These results indicate that the intrinsic protein kinase activity of cerebral membrane fragments is due to the presence of a kinase enzyme which is specific to certain membrane proteins. The intrinsic protein kinase activity of synaptosome membrane fragments is a rather slow reaction which takes several minutes to saturate all the acceptor proteins.
已对大脑中组蛋白和磷蛋白激酶活性的亚细胞分布进行了研究，并且还检测了各个组分催化其内源性蛋白质磷酸化的能力（内在蛋白激酶活性）。突触体膜碎片几乎没有组蛋白或磷蛋白激酶活性，但含有最高浓度的环磷酸腺苷刺激的内在蛋白激酶活性。用曲拉通X-100对膜碎片进行匀浆可增加组蛋白激酶活性，但离心后其全部在上清液中回收，而不溶性物质则含有所有的内在蛋白激酶活性。这些结果表明，脑膜碎片的内在蛋白激酶活性是由于存在一种对某些膜蛋白具有特异性的激酶。突触体膜碎片的内在蛋白激酶活性是一个相当缓慢的反应，需要几分钟才能使所有受体蛋白饱和。
