Brady S T, Tytell M, Lasek R J
J Cell Biol. 1984 Nov;99(5):1716-24. doi: 10.1083/jcb.99.5.1716.
Nerve extracts containing tubulin labeled by axonal transport were analyzed by electrophoresis and differential extraction. We found that a substantial fraction of the tubulin in the axons of the retinal ganglion cell of guinea pigs is not solubilized by conventional methods for preparation of microtubules from whole brain. In two-dimensional polyacrylamide gel electrophoresis this cold-insoluble tubulin was biochemically distinct from tubulin obtained from whole brain microtubules prepared by cold cycling. Cleveland peptide maps also indicated some differences between the cold-extractable and cold-insoluble tubulins. The demonstration of cold-insoluble tubulin that is specifically axonal in origin permits consideration of the physiological role of cold-insoluble tubulin in a specific cellular structure. It appears likely that much of this material is in the form of cold-stable microtubules. We propose that the physiological role of cold-insoluble tubulin in the axon may be associated with the regulation of the axonal microtubule complexes in neurons.
通过电泳和差异提取对含有经轴突运输标记微管蛋白的神经提取物进行了分析。我们发现，豚鼠视网膜神经节细胞轴突中的很大一部分微管蛋白不能通过从全脑制备微管的传统方法溶解。在二维聚丙烯酰胺凝胶电泳中，这种冷不溶性微管蛋白在生化性质上与通过冷循环从全脑微管中获得的微管蛋白不同。克利夫兰肽图也表明冷可提取和冷不溶性微管蛋白之间存在一些差异。对起源于特定轴突的冷不溶性微管蛋白的证明，使得我们能够考虑冷不溶性微管蛋白在特定细胞结构中的生理作用。看起来这种物质的大部分是以冷稳定微管的形式存在。我们提出，轴突中冷不溶性微管蛋白的生理作用可能与神经元中轴突微管复合体的调节有关。
