首页> 美国卫生研究院文献>Proceedings of the National Academy of Sciences of the United States of America >12-fold difference between the critical monomer concentrations of the two ends of actin filaments in physiological salt conditions.
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12-fold difference between the critical monomer concentrations of the two ends of actin filaments in physiological salt conditions.

机译:在生理盐条件下肌动蛋白丝两端的关键单体浓度之间存在12倍的差异。

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摘要

We determined the critical monomer concentrations at which association and dissociation reactions are balanced at the two ends of actin filaments. For measurement of the critical concentration of the pointed end, interference with the high dynamics of the barbed end was excluded by capping the barbed ends with an actin filament capping protein isolated from bovine brain. The critical concentration of the pointed end (1.5 microM) was found to be 12- to 15-fold higher than the critical concentration of the barbed end (0.10-0.12 microM) at a temperature of 37 degrees C and physiological salt concentrations (100 mM KCl/1-2 mM MgCl2/0.3 mM EGTA or 0.2 mM CaCl2, pH 7.5).
机译:我们确定了肌动蛋白丝两端的缔合和解离反应平衡的临界单体浓度。为了测量尖端的临界浓度,通过用从牛脑分离的肌动蛋白丝加帽蛋白加帽,将对有刺端的高动态干扰排除在外。在37摄氏度的温度和生理盐浓度(100 mM)下,尖端的临界浓度(1.5 microM)比带刺的末端的临界浓度(0.10-0.12 microM)高12至15倍KCl / 1-2 mM MgCl2 / 0.3 mM EGTA或0.2 mM CaCl2,pH 7.5)。

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