Schmidt J M, Robson R M, Zhang J, Stromer M H
Department of Biochemistry and Biophysics, Iowa State University, Ames 50011.
Biochem Biophys Res Commun. 1993 Dec 15;197(2):660-6. doi: 10.1006/bbrc.1993.2530.
The effect of pH on the interaction between talin and actin was examined by using cosedimentation assays, low shear viscometry, and electron microscopy. When the pH at which the interaction was tested was lowered from 7.5 to 7.0 and below, the ability of talin to cosediment with F-actin was greatly enhanced, with maximal binding at pH 6.6. Talin's ability to increase the low shear viscosity of F-actin solutions was also significantly elevated as pH was decreased from 7.4 to 6.6. Electron microscope observations of negatively stained actin controls and talin-actin mixtures supported these results by demonstrating an increase in the degree of crosslinking of actin filaments in the presence of talin at pH values of 7 and lower.
通过使用共沉降分析、低剪切粘度测定法和电子显微镜,研究了pH对踝蛋白与肌动蛋白之间相互作用的影响。当测试相互作用时的pH从7.5降至7.0及以下时,踝蛋白与F-肌动蛋白共沉降的能力大大增强,在pH 6.6时结合力最大。随着pH从7.4降至6.6,踝蛋白增加F-肌动蛋白溶液低剪切粘度的能力也显著提高。对负染色的肌动蛋白对照和踝蛋白-肌动蛋白混合物的电子显微镜观察支持了这些结果,表明在pH值为7及更低时,在踝蛋白存在下肌动蛋白丝的交联程度增加。