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F-肌动蛋白流变学特性的物理基础。

Physical basis of the rheologic properties of F-actin.

作者信息

Zaner K S, Stossel T P

出版信息

J Biol Chem. 1983 Sep 25;258(18):11004-9.

PMID:6885809
Abstract

The viscoelastic properties of purified rabbit skeletal muscle actin filaments (F-actin) were measured at physiologic ionic strength and pH over a range of concentrations and filament lengths. Although F-actin demonstrated transitory elastic behavior, viscous flow was observed at longer times consistent with a high degree of filament overlap. The compliance was independent of stress over a 4-fold range, implying that the measurement did not disrupt any interfilament "bonds". The dynamic storage modulus increased monotonically with frequency over the range measured, whereas the dynamic loss modulus had a relative minimum and was always less than the dynamic storage modulus. These observations are typical of topologically constrained behavior. The absolute value of the complex dynamic viscosity of F-actin, varied as the -0.8 power of the frequency and at a frequency of 0.1 radians/s was proportional to the product of the weight average filament length raised to the 0.7 power and the concentration. The experimental data agreed well with the predictions of a theory of the rheologic behavior of stiff rods in semidilute solutions. We conclude that the mechanical behavior of pure F-action solutions can be explained on the basis of the mutual topologic constraints to diffusion of long stiff rods which do not otherwise interact.

摘要

在生理离子强度和pH值条件下,在一系列浓度和细丝长度范围内,对纯化的兔骨骼肌肌动蛋白细丝(F-肌动蛋白)的粘弹性特性进行了测量。尽管F-肌动蛋白表现出短暂的弹性行为,但在较长时间观察到粘性流动,这与高度的细丝重叠一致。在4倍的范围内,顺应性与应力无关,这意味着测量并未破坏任何细丝间的“键”。在所测量的频率范围内,动态储能模量随频率单调增加,而动态损耗模量有一个相对最小值,且始终小于动态储能模量。这些观察结果是拓扑约束行为的典型特征。F-肌动蛋白的复数动态粘度绝对值随频率的-0.8次方变化,在0.1弧度/秒的频率下,与重均细丝长度的0.7次方和浓度的乘积成正比。实验数据与半稀溶液中刚性棒流变行为理论的预测结果吻合良好。我们得出结论,纯F-肌动蛋白溶液的力学行为可以基于长刚性棒扩散的相互拓扑约束来解释,这些刚性棒在其他方面不相互作用。

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