Magilen G, Gordon A, Au A, Diamond I
J Neurochem. 1981 May;36(5):1861-4. doi: 10.1111/j.1471-4159.1981.tb00442.x.
A 41,000-dalton phosphoprotein in crude synaptosomal membrane fractions is characterized by its unique divalent and monovalent cation regulation. It is identified by two-dimensional gel electrophoresis as the phosphoprotein whose phosphorylation is enhanced by repetitive electrical stimulation of hippocampal brain slices. After sucrose-gradient ultracentrifugation, this phosphoprotein is found in the mitochondrial subfraction. This suggests that the electrically produced changes in the level of phosphorylation of the 41,000-dalton polypeptide are probably effects on cellular energetics rather than on specialized neural membrane function.
粗制突触体膜组分中的一种41000道尔顿的磷蛋白，其特征在于独特的二价和单价阳离子调节。通过二维凝胶电泳鉴定，它是一种磷蛋白，海马脑片的重复电刺激可增强其磷酸化。经蔗糖梯度超速离心后，这种磷蛋白存在于线粒体亚组分中。这表明，电刺激产生的41000道尔顿多肽磷酸化水平变化可能是对细胞能量代谢的影响，而非对特殊神经膜功能的影响。
