用动力学方法分析细丝蛋白与肌动蛋白的结合及交联/成束作用。

Analysis of filamin-actin binding and cross-linking/bundling by kinetic method.

作者信息

Goldmann W H, Senger R, Isenberg G

机构信息

Technical University of Munich, Garching, FRG.

出版信息

Biochem Biophys Res Commun. 1994 Aug 30;203(1):338-43. doi: 10.1006/bbrc.1994.2187.

DOI:10.1006/bbrc.1994.2187

PMID:8074676

Abstract

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.

摘要

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。