Kiaĭviariaĭnen A I
Biofizika. 1978 Jul-Aug;23(4):595-601.
The effect of NaCl, (NH4)2SO4, sodium dodecylsulphate and temperature on conformational properties of light-chain dimers and the Fab-fragments of immunoglobulins G has been investigated using the spin-label method. All these agents despite their different nature, induce qualitatively the same shift in the equilibrium between the A- and B-states of spin label towards the state of higher microviscosity A. The effect of 1.2 M NaCl and 0.75 M (NH4)2SO4 increase the stability of IgG in relation to temperature, as a result of this shift. The data obtained are interpreted in terms of the dynamic model of protein behaviour in water suggested earlier. In accordance with the model the action of the agents perturbing the conformation of protein and the ordered structure of water in the non-polar cavities of protein, reduce the life-time of this cavities in the water accessible state.
采用自旋标记法研究了氯化钠、硫酸铵、十二烷基硫酸钠和温度对免疫球蛋白G轻链二聚体和Fab片段构象性质的影响。所有这些试剂尽管性质不同，但在定性上都会使自旋标记物A态和B态之间的平衡朝着更高微粘度的A态发生相同的移动。由于这种移动，1.2M氯化钠和0.75M硫酸铵的作用提高了IgG相对于温度的稳定性。根据先前提出的蛋白质在水中行为的动力学模型对所得数据进行了解释。根据该模型，干扰蛋白质构象和蛋白质非极性腔中水的有序结构的试剂的作用，缩短了这些腔在水可及状态下的寿命。
