Millar N C, Geeves M A
FEBS Lett. 1983 Aug 22;160(1-2):141-8. doi: 10.1016/0014-5793(83)80954-5.
The ATP-induced dissociation of actoS1 has been studied at temperatures between -10 degrees C and +30 degrees C in a stopped-flow apparatus using ethylene glycol as antifreeze. At temperatures at and below 0 degrees C the observed rate of the dissociation of actin shows a hyperbolic dependence on ATP concentration. This is interpreted in terms of a rapid binding of ATP followed by an isomerisation of the ternary complex which results in actin dissociation. Ethylene glycol weakens ATP binding but the rate of the isomerisation is unaffected. The second order rate constant for the dissociation shows a break in the Arrhenius plot.
在使用乙二醇作为防冻剂的停流装置中，研究了在-10℃至+30℃之间的温度下ATP诱导的肌动蛋白S1解离。在0℃及以下温度时，观察到的肌动蛋白解离速率对ATP浓度呈双曲线依赖关系。这可以解释为ATP快速结合，随后三元复合物发生异构化，导致肌动蛋白解离。乙二醇会削弱ATP结合，但异构化速率不受影响。解离的二级速率常数在阿仑尼乌斯图上出现转折。
