Sandvold M L, Mikkelsen A, Elgsaeter A
Department of Physics and Mathematics, Norwegian Institute of Technology, University of Trondheim.
Acta Chem Scand (Cph). 1989 Sep;43(8):783-6. doi: 10.3891/acta.chem.scand.43-0783.
The frequency dependence (119-7860 Hz) of the storage and loss shear moduli, G' and G'', of human erythrocyte spectrin dimer crude solutions at 22.5 degrees C has been measured using a Birnboim-Schrag multiple lumped resonator viscoelastometer. The measurements were carried out on solutions of ionic strength 1 mM containing 1.1-3.7 mg ml-1 spectrin. This corresponds to the terminal zone for G' and G''. Analysis of the data using the standard theory of hybrid relaxation spectra yields a relaxation time of 22.5 +/- 1 microseconds. The pure spectrin dimer relaxation time is estimated to be 16 +/- 3 microseconds. This result suggests that at an ionic strength of 1 mM, the spectrin dimers are extended and that the main relaxation process is simple end-over-end rotation.
在22.5摄氏度下,使用Birnboim-Schrag多集总谐振器粘弹性计测量了人红细胞血影蛋白二聚体粗溶液的储能剪切模量G'和损耗剪切模量G''的频率依赖性(119 - 7860赫兹)。测量是在离子强度为1 mM、含有1.1 - 3.7 mg/ml血影蛋白的溶液上进行的。这对应于G'和G''的终端区。使用混合弛豫谱的标准理论对数据进行分析,得到弛豫时间为22.5±1微秒。纯血影蛋白二聚体的弛豫时间估计为16±3微秒。该结果表明,在离子强度为1 mM时,血影蛋白二聚体是伸展的,并且主要弛豫过程是简单的端对端旋转。