Goldmann W H, Senger R, Isenberg G
Technical University of Munich, Garching, FRG.
Biochem Biophys Res Commun. 1994 Aug 30;203(1):338-43. doi: 10.1006/bbrc.1994.2187.
The reaction of smooth muscle filamin and skeletal muscle actin was kinetically examined by double exponential analysis. The overall rate of binding, k+1, is concentration and temperature dependent whilst the overall rate of cross-linking/bundling, k+2, is concentration independent. The activation energy, Ea = 99.5 kJ/mol, was calculated from the Arrhenius Plot.
通过双指数分析对平滑肌细丝蛋白与骨骼肌肌动蛋白的反应进行了动力学研究。结合的总速率k+1取决于浓度和温度，而交联/成束的总速率k+2与浓度无关。根据阿伦尼乌斯曲线计算出活化能Ea = 99.5 kJ/mol。
