Karr T L, Kristofferson D, Purich D L
J Biol Chem. 1980 Sep 25;255(18):8560-6.
Microtubule disassembly has been studied using a rapid dilution technique (Karr, T.L., and Purich, D.L. (1979) J. Biol. Chem. 254, 10885-10888). Disassembly curves, generated by computer from the solution of series first order differential equations (see following paper), were fit to experimental data with excellent agreement when the diluted microtubules contained no microtubule-associated proteins. The rate constant for dimer release from microtubules was found to be 154 s-1. Assuming a critical tubulin concentration of 8 to 9 x 10(-6) M, the apparent bimolecular rate constant (2 x 10(7) M-1 s-1) for assembly is near the diffusion limit. It was also possible to use the rapid dilution technique for quantitatively correlating the disassembly rate to the number concentration of microtubule ends. These findings suggest that the dynamics of tubulin interactions with microtubules may be characterized in terms of an endwise depolymerization model. A re-evaluation of cold induced depolymerization kinetics (see miniprint supplement) is also fully consistent with our analysis of disassembly dynamics.
微管解聚已通过快速稀释技术进行了研究（卡尔，T.L.，和普里希，D.L.（1979年）《生物化学杂志》254，10885 - 10888）。当稀释的微管中不含有微管相关蛋白时，由计算机从一系列一阶微分方程的解生成的解聚曲线与实验数据拟合得非常好。发现微管中二聚体释放的速率常数为154 s⁻¹。假设微管蛋白的临界浓度为8至9×10⁻⁶ M，组装的表观双分子速率常数（2×10⁷ M⁻¹ s⁻¹）接近扩散极限。还可以使用快速稀释技术将解聚速率与微管末端的数量浓度进行定量关联。这些发现表明，微管蛋白与微管相互作用的动力学可以用末端解聚模型来描述。对冷诱导解聚动力学的重新评估（见缩印补充材料）也与我们对解聚动力学的分析完全一致。
