Tashiro T, Kurokawa M, Komiya Y
J Neurochem. 1984 Nov;43(5):1220-5. doi: 10.1111/j.1471-4159.1984.tb05376.x.
In the sensory fibers of the rat sciatic nerve (fibers of the dorsal root ganglion cells), two components of tubulin transport were observed that differed in the rate of transport, solubility in Triton, and subunit composition. The faster component, migrating ahead of the neurofilament proteins, was soluble in 1% Triton. The slower component, migrating with the neurofilament proteins, was insoluble in 1% Triton and contained a unique polypeptide, "NAP," in the tubulin region that was not present in the faster component. "NAP" was not a subspecies of tubulin as evidenced by peptide mapping. It seems to be a neurofilament-associated protein. When a complete separation of the main tubulin wave from the neurofilament wave was achieved in the motor axons of the same nerve (axons of the ventral motoneurons) under the effect of beta,beta'-iminodipropionitrile, a portion of tubulin was still found associated with the retarded neurofilament wave. The subunit composition of this portion was similar to the slower, neurofilament-associated component in the sensory fibers under normal conditions, i.e., enriched in "NAP" and the most acidic subtype of beta-tubulin. It is suggested that two populations of transported tubulin exist that are differentiated by the extent of their interaction with neurofilaments.
在大鼠坐骨神经的感觉纤维（背根神经节细胞的纤维）中，观察到微管蛋白运输的两个组分，它们在运输速率、在曲拉通中的溶解度和亚基组成方面存在差异。较快的组分在神经丝蛋白之前迁移，可溶于1%的曲拉通。较慢的组分与神经丝蛋白一起迁移，不溶于1%的曲拉通，并且在微管蛋白区域含有一种独特的多肽“NAP”，而较快的组分中不存在这种多肽。肽图谱分析表明，“NAP”不是微管蛋白的一个亚种。它似乎是一种与神经丝相关的蛋白。当在β,β'-亚氨基二丙腈的作用下，在同一条神经的运动轴突（腹侧运动神经元的轴突）中实现微管蛋白主波与神经丝波的完全分离时，仍发现一部分微管蛋白与延迟的神经丝波相关。这部分的亚基组成与正常条件下感觉纤维中较慢的、与神经丝相关的组分相似，即富含“NAP”和β-微管蛋白的最酸性亚型。有人提出，存在两种运输的微管蛋白群体，它们通过与神经丝相互作用的程度而区分开来。
