Vale R D, Reese T S, Sheetz M P
Cell. 1985 Aug;42(1):39-50. doi: 10.1016/s0092-8674(85)80099-4.
Axoplasm from the squid giant axon contains a soluble protein translocator that induces movement of microtubules on glass, latex beads on microtubules, and axoplasmic organelles on microtubules. We now report the partial purification of a protein from squid giant axons and optic lobes that induces these microtubule-based movements and show that there is a homologous protein in bovine brain. The purification of the translocator protein depended primarily on its unusual property of forming a high affinity complex with microtubules in the presence of a nonhydrolyzable ATP analog, adenylyl imidodiphosphate. The protein, once released from microtubules with ATP, migrates on gel filtration columns with an apparent molecular weight of 600 kilodaltons and contains 110-120 and 60-70 kilodalton polypeptides. This protein is distinct in molecular weight and enzymatic behavior from myosin or dynein, which suggests that it belongs to a novel class of force-generating molecules, for which we propose the name kinesin.
枪乌贼巨大轴突的轴浆中含有一种可溶性蛋白质转运体，它能促使微管在玻璃上移动、微管上的乳胶珠移动以及微管上的轴浆细胞器移动。我们现在报告从枪乌贼巨大轴突和视叶中部分纯化出一种能引发这些基于微管运动的蛋白质，并表明牛脑中存在一种同源蛋白质。转运体蛋白的纯化主要依赖于其在不可水解的ATP类似物腺苷酰亚胺二磷酸存在下与微管形成高亲和力复合物的特殊性质。该蛋白质一旦在ATP作用下从微管上释放，在凝胶过滤柱上迁移时的表观分子量为600千道尔顿，包含110 - 120千道尔顿和60 - 70千道尔顿的多肽。这种蛋白质在分子量和酶促行为上与肌球蛋白或动力蛋白不同，这表明它属于一类新型的产生力的分子，我们为此提议将其命名为驱动蛋白。
