Goldmann W H, Tempel M, Sprenger I, Isenberg G, Ezzell R M
Surgery Research Laboratories, Massachusetts General Hospital, Harvard Medical School, Charlestown 02129, USA.
Eur J Biochem. 1997 Jun 1;246(2):373-9. doi: 10.1111/j.1432-1033.1997.00373.x.
Cross-linking of actin filaments by filamin by means of frequency-dependent rheology yields an increase in the filament's elasticity and stiffness. Higher cross-linker (filamin) ratios are required for mean actin-filament lengths of 5-6 microm than for random-length distribution of actin filaments. The loss modulus (i.e. the viscous portion) in the region of the internal-chain dynamics [G"(omega) approximately omega(alpha)] is influenced by the cross-linking of filaments, and with an increasing molar ratio of filamin/actin a reduction of alpha is observed. Rheological measurements reveal that actin networks are already formed at the polymerizing stage at a molar ratio of filamin/actin of less than 1:100, and electron micrographs show phase separation of actin/filament networks of low density and of actin/filament bundles.
通过频率依赖性流变学，细丝蛋白使肌动蛋白丝交联，从而增加了肌动蛋白丝的弹性和刚度。与肌动蛋白丝随机长度分布相比，平均肌动蛋白丝长度为5 - 6微米时需要更高的交联剂（细丝蛋白）比例。内链动力学区域的损耗模量（即粘性部分）[G"(ω) 近似于 ω(α)] 受细丝交联的影响，随着细丝蛋白/肌动蛋白摩尔比的增加，α 减小。流变学测量表明，在聚合阶段，细丝蛋白/肌动蛋白摩尔比小于1:100时就已形成肌动蛋白网络，电子显微镜照片显示了低密度的肌动蛋白/细丝网络和肌动蛋白/细丝束的相分离。
