INTERACTION OF CALF BRAIN TUBULIN WITH GLYCEROL
INTERACTION OF CALF BRAIN TUBULIN WITH GLYCEROL
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DOI：
10.1016/0022-2836(81)90226-6
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发表时间：
1981-01-01
影响因子：
5.6
通讯作者：
TIMASHEFF, SN
中科院分区：
文献类型：
--
作者：
NA, GC;TIMASHEFF, SN
在0.01 m-NaP i, 0.02 m-NaCl, 10−4 m-GTP, pH 7.0的缓冲液中，用密度法研究了小牛脑微管蛋白与甘油的优先相互作用。在0、10、20和30%（v / v）甘油条件下，测定了微管蛋白在恒定化学势下的表观比体积。多组分溶液热力学的应用表明，微管蛋白在甘油水溶液中优先水化，这种相互作用通过提高甘油和微管蛋白的化学势导致系统的热力学不稳定。根据Wyman键函数解释，蛋白质-甘油优先相互作用带来的不利自由能变化可以解释甘油增强微管蛋白在体外自组装成微管的原因，并为甘油稳定天然微管蛋白构象提供了基本原理。
The preferential interaction of calf brain tubulin with glycerol in an aqueous buffer (0.01 m-NaP i, 0.02 m-NaCl, 10− 4 m-GTP, pH 7.0) has been investigated by densimetry. The apparent specific volumes of tubulin at constant chemical potential of the diffusible components were determined at 0, 10, 20 and 30%(v v) glycerol. Application of multicomponent solution thermodynamics shows that tubulin is preferentially hydrated in aqueous glycerol solvent and that such interaction results in thermodynamic destabilization of the system by raising the chemical potentials of both glycerol and tubulin. Interpreted in terms of the Wyman linkage function, the unfavorable free energy change brought about by the preferential protein-glycerol interaction can account for the glycerol enhancement of tubulin self-assembly in vitro into microtubules as well as offer a rationale for glycerol stabilization of the native tubulin conformation.