Zaner K S, Stossel T P
J Cell Biol. 1982 Jun;93(3):987-91. doi: 10.1083/jcb.93.3.987.
Measurements of the dynamic viscosity of various actin filament preparations under conditions of low and controlled shear: (a) confirm the shear rate dependence of F-actin viscosities and show that this dependence obeys the power law relationship observed for entangled synthetic polymers; (b) permit estimation of the extent to which shear artifact amplifies changes in the apparent viscosity of F-actin measured in a falling ball viscometer; (c) show that gel-filtration chromatography of actin and the addition of cytochalasin B to F-actin bring about small (20-40%) changes in the viscosity of the F-actin solutions. These variations are consistent with alterations in the actin-binding protein concentrations required for incipient gelation, a parameter inversely related to average filament length. Therefore: (a) changes in the viscosity of F-actin can be magnified by use of the falling ball viscometer, and may exaggerate their biological importance; (b) chromatography of actin may not be required to obtain meaningful information about the rheology of actin filaments; (c) changes in actin filament length can satisfactorily explain alterations in F-actin viscosity exerted by cytochalasin B and by chromatography, obviating the need to postulate specific interfilament interactions.
在低剪切力且可控的条件下,对各种肌动蛋白丝制剂的动态粘度进行测量:(a) 证实了F-肌动蛋白粘度对剪切速率的依赖性,并表明这种依赖性符合在缠结合成聚合物中观察到的幂律关系;(b) 可以估计在落球粘度计中测量F-肌动蛋白表观粘度时,剪切伪像放大变化的程度;(c) 表明肌动蛋白的凝胶过滤色谱法以及向F-肌动蛋白中添加细胞松弛素B会使F-肌动蛋白溶液的粘度发生小幅度(20%-40%)变化。这些变化与初始凝胶化所需的肌动蛋白结合蛋白浓度的改变一致,该参数与平均丝长度呈反比关系。因此:(a) 使用落球粘度计可放大F-肌动蛋白的粘度变化,并可能夸大其生物学重要性;(b) 可能不需要对肌动蛋白进行色谱分析就能获得有关肌动蛋白丝流变学的有意义信息;(c) 肌动蛋白丝长度的变化可以令人满意地解释细胞松弛素B和色谱法对F-肌动蛋白粘度的改变,从而无需假设特定的丝间相互作用。