Analytical Sciences, Amgen, Inc., 4000 Nelson Road, Longmont, Colorado 80503, USA.
Anal Chem. 2010 Feb 1;82(3):1090-9. doi: 10.1021/ac902466z.
The detection and characterization of unexpected disulfide-mediated structural variants of human immunoglobulin G2 (IgG2) antibodies was recently the subject of two copublications. In this paper, we present data to confirm the previously reported structures and elucidate the complete disulfide connectivity of each variant through the application of a novel analytical methodology. In this manner, the data illustrate the presence of at least five structural variants, including the classical structure with independent Fab domains and a hinge region. Multiple subvariants of the IgG2-A/B and IgG2-B structures are identified; these subvariants of each structure differ through the order of attachment of Fab peptides to the sequential hinge cysteines. Furthermore, the connectivity of a novel subvariant of IgG2-B containing an intrachain disulfide linkage in the lower hinge region is elucidated. The results presented in this paper reveal that the population of IgG2 disulfide structural variants is yet more complex than recently reported.
最近有两篇共同发表的文章探讨了人免疫球蛋白 G2（IgG2）抗体中意外的二硫键介导的结构变异的检测和特征分析。本文通过应用一种新的分析方法，提供了数据来证实之前报道的结构，并阐明了每个变体的完整二硫键连接。通过这种方式，数据表明至少存在五种结构变体，包括具有独立 Fab 结构域和铰链区的经典结构。鉴定出 IgG2-A/B 和 IgG2-B 结构的多个亚变体；这些结构的每个亚变体通过 Fab 肽连接到顺序铰链半胱氨酸的顺序而有所不同。此外，阐明了含有铰链区中下铰链区域内链间二硫键连接的新型 IgG2-B 亚变体的连接性。本文介绍的结果表明，IgG2 二硫键结构变体的群体比最近报道的更为复杂。
