Boyar M M, Coutinho-Netto J, Abdul-Ghani A S, Bradford H F
J Neurochem. 1981 Dec;37(6):1371-6. doi: 10.1111/j.1471-4159.1981.tb06304.x.
The incorporation of [U-14C] protein hydrolysate and [U-14C]leucine into the trichloroacetic acid (TCA)-insoluble membrane and the soluble synaptoplasm proteins of synaptosomes was studied. Following treatment with the depolarizing agents veratrine, Tityus toxin, or potassium, the specific radioactivity of both precursor pool and proteins were measured to examine the link between protein labeling and the fall in the free amino acid pool due to depolarization-induced release of glutamate and aspartate. By reducing the size of the fall in precursor pool due to depolarization by using a nontransmitter amino acid such as leucine (as compared with the usual use of protein hydrolysate), it was shown that the amount of which the pool is reduced is proportional to the change in the protein labeling observed. These results confirm that membrane depolarization causes a large increase in the labeling of membrane-bound proteins as compared with the soluble synaptosomal proteins.
研究了[U-14C]蛋白水解物和[U-14C]亮氨酸掺入突触体的三氯乙酸（TCA）不溶性膜和可溶性突触浆蛋白中的情况。在用去极化剂藜芦碱、Tityus毒素或钾处理后，测量前体池和蛋白质的比放射性，以检查蛋白质标记与由于去极化诱导的谷氨酸和天冬氨酸释放导致的游离氨基酸池下降之间的联系。通过使用非递质氨基酸如亮氨酸（与通常使用的蛋白水解物相比）来减少由于去极化导致的前体池下降的幅度，结果表明前体池减少的量与观察到的蛋白质标记变化成正比。这些结果证实，与可溶性突触体蛋白相比，膜去极化会导致膜结合蛋白的标记大幅增加。
