Białkowska H, Morawiecki A
Arch Immunol Ther Exp (Warsz). 1978;26(1-6):133-8.
The interaction of rabbit non-specific IgG and human erythrocyte glycoprotein was investigated using the solvent perturbation difference spectroscopy method. This interaction manifested itself by decreasing accessibility of chromophores to perturbants. Masking of the chromophores was abolished by low detergent concentrations and by changes of native IgG structure by 3 M urea. The sialic acid residues of the glycoprotein were necessary for this effect but probably not due to simple electrostatic interactions. It seems that the IgG-glycoprotein interaction requires intact both--the IgG molecule structure and the structure of the glycoprotein micelle. Interaction of this kind was not observed between glycoprotein and some other proteins as bovine serum albumin, alpha-chymotrypsynogen and human IgA.
采用溶剂扰动差示光谱法研究了兔非特异性IgG与人红细胞糖蛋白的相互作用。这种相互作用表现为发色团对扰动剂的可及性降低。低浓度去污剂以及3M尿素改变天然IgG结构可消除发色团的掩蔽作用。糖蛋白的唾液酸残基对这种效应是必需的，但可能并非简单的静电相互作用所致。似乎IgG与糖蛋白的相互作用要求IgG分子结构和糖蛋白微团结构均保持完整。在糖蛋白与其他一些蛋白质如牛血清白蛋白、α-胰凝乳蛋白酶原和人IgA之间未观察到这种相互作用。
