Zav'yalov V P, Tetin S Y, Abramov V M, Troitsky G V
Biochim Biophys Acta. 1978 Apr 26;533(2):496-503. doi: 10.1016/0005-2795(78)90395-1.
An effect of salt concentration on the human myeloma immunoglobulin G structure was studied by means of circular dichroism, thermal perturbation difference spectroscopy and isoelectric focusing in a pH gradient created by a concentration gradient of glucose in borate buffer solution. Immunoglobulin G (K) Iva showed a significant shift of isoelectric point to the alkaline region as a result of the increase in salt concentration. The difference spectra indicated a change in the exposure of tyrosine residues as a result of increase in salt concentration. No changes in the circular dichroic spectra with salt concentration were observed between 205 and 250 nm. Spectral changes observed for the undigested immunoglobulin G molecule are more marked than those observed for the isolated Fab fragments.
通过圆二色性、热扰动差光谱法以及在硼酸盐缓冲溶液中由葡萄糖浓度梯度产生的pH梯度下的等电聚焦,研究了盐浓度对人骨髓瘤免疫球蛋白G结构的影响。免疫球蛋白G(K)Iva显示,由于盐浓度的增加,等电点显著向碱性区域移动。差光谱表明,由于盐浓度的增加,酪氨酸残基的暴露情况发生了变化。在205至250纳米之间,未观察到圆二色光谱随盐浓度的变化。未消化的免疫球蛋白G分子观察到的光谱变化比分离的Fab片段观察到的更明显。