肌原溶酶存在下Ca2+诱导的肌动蛋白疟原虫聚合物构象变化。

H Tanaka, S Hatano
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引用次数: 0

摘要

肌动蛋白plasmodium actin的柔性聚合物(Mg-polymer)与肌肉天然原肌凝蛋白结合,达到肌动蛋白:原肌凝蛋白:肌钙蛋白的重量比= 6:1:1。当加入0.5 mM乙二醇双(β -氨基乙醚)-N,N'-四乙酸(EGTA)降低溶液中Ca2+浓度时,mg -聚合物与肌肉天然原肌球蛋白结合后发生构象变化:溶液粘度增加50%,atp酶活性下降到原值的20%左右,表明mg -聚合物的结构变得更加刚性。溶液中Ca2+浓度的变化是可逆的。构象变化的Ca2+阈值浓度约为10(-6)m,并讨论了这种转化在体内的可能作用。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Conformational changes induced in plasmodium actin polymer by Ca2+ in the presence of muscle native tropomysin.

The flexible polymer of plasmodium actin (Mg-polymer) combines with muscle native tropomyosin up to a weight ratio of actin: tropomyosin:troponin = 6:1:1. Mg-polymer which combined with muscle native tropomyosin undergoes a conformational change when the Ca2+ concentration of the solution is decreased by adding 0.5 mM ethylene glycol bis(beta-aminoethylether)-N,N'-tetraacetic acid (EGTA): the viscosity of the solution increases by 50% and its ATPase activity decreases to about 20% of the original value, which suggests that the structure of Mg-polymer becomes more rigid. This change is reversible with respect to the Ca2+ concentration in the solution. The threshold concentration of Ca2+ for the conformational change is about 10(-6) M. The possible role of this transformation in vivo is discussed.

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