Menon R S, Allen P S
Department of Applied Sciences in Medicine, University of Alberta, Edmonton, Canada.
Biophys J. 1990 Mar;57(3):389-96. doi: 10.1016/S0006-3495(90)82555-8.
The longitudinal, transverse, and spin-locked rotating frame relaxation rates have been measured for water protons in aqueous solutions of the human serum proteins albumin, fibrinogen, and alpha 2-macroglobulin in the physiological concentration range below 50 g/liter, corresponding to an upper limit for molarity of 725, 147, and 69 microM, respectively. The linear concentration dependence of all the relaxation rates measured at 100 MHz was used to provide the molar sensitivities of each relaxation process for each of the protein solutes. Both the solute dependence and the relaxation-process dependence of the molar sensitivities have been analyzed in terms of a model that has emerged from previous R1 dispersion measurements. This analysis demonstrates consistency between our data and that model for the active motions and their motional rates.
已测量了人血清蛋白白蛋白、纤维蛋白原和α2-巨球蛋白在生理浓度范围（低于50 g/升，分别对应摩尔浓度上限725、147和69 μM）的水溶液中水质子的纵向、横向和自旋锁定旋转框架弛豫率。利用在100 MHz下测量的所有弛豫率的线性浓度依赖性，得出了每种蛋白质溶质各弛豫过程的摩尔灵敏度。根据先前R1色散测量得出的模型，分析了摩尔灵敏度的溶质依赖性和弛豫过程依赖性。该分析表明，我们的数据与该模型在活性运动及其运动速率方面具有一致性。
