Shimizu M, Nagashima H, Sano K, Hashimoto K, Ozeki M, Tsuda K, Hatta H
School of Food and Nutritional Sciences, University of Shizuoka, Japan.
Biosci Biotechnol Biochem. 1992 Feb;56(2):270-4. doi: 10.1271/bbb.56.270.
Molecular stability of chicken egg yolk immunoglobulin G (IgY) and that of rabbit IgG were compared by measuring antibody activities and conformational changes. Stability of rabbit IgG to acid denaturation was much higher than that of IgY. Conformation of the IgY molecule was readily changed in acidic conditions, resulting in a rapid loss of antibody activity. Much less stable natures of IgY to heat-treatment and guanidine-HCl denaturation than rabbit IgG were also observed. Differences in the structure between the two immunoglobulins that might participate in their different stability were inferred from their amino acid sequence data. Importance of the intramolecular disulfide linkage in the rabbit light chain and some other structural differences were suggested.
通过测量抗体活性和构象变化，比较了鸡卵黄免疫球蛋白G（IgY）和兔免疫球蛋白G（IgG）的分子稳定性。兔IgG对酸变性的稳定性远高于IgY。IgY分子的构象在酸性条件下很容易改变，导致抗体活性迅速丧失。还观察到IgY对热处理和盐酸胍变性的稳定性远低于兔IgG。从它们的氨基酸序列数据推断出两种免疫球蛋白之间可能参与其不同稳定性的结构差异。提示了兔轻链中分子内二硫键的重要性以及其他一些结构差异。
