Peppard J V, Hobbs S M, Jackson L E
Department of Immunology and Microbiology, Wayne State University School of Medicine, Detroit, MI 48201.
Mol Immunol. 1989 May;26(5):495-500. doi: 10.1016/0161-5890(89)90109-0.
Monoclonal IgG1, IgG2a, IgG2b and IgG2c were prepared from rat hybridoma cells treated with tunicamycin in order to inhibit N-linked glycosylation. The IgG produced by these cells was about 70% lower in carbohydrate content compared to IgG from equivalent untreated cells, but was similar to the corresponding normal IgG in terms of antigen binding. However, the ability of carbohydrate deficient (CHO-) IgG to bind in vitro to Fc receptor extracted from jejunum of neonatal rats was impaired in most cases and, in all but one case, the amount of CHO- IgG transported from gut lumen to blood in vivo was markedly reduced. No reduction in binding of normal IgG to extracted receptor was observed in the presence of various sugars. It is postulated that N-linked carbohydrate acts to stabilize the structure within the IgG molecule which is responsible for binding to this Fc receptor, possibly in the CH2 domain.
制备了单克隆IgG1、IgG2a、IgG2b和IgG2c，其来源于用衣霉素处理的大鼠杂交瘤细胞，目的是抑制N-连接糖基化。与未处理的同等细胞产生的IgG相比，这些细胞产生的IgG碳水化合物含量降低了约70%，但在抗原结合方面与相应的正常IgG相似。然而，在大多数情况下，碳水化合物缺陷型（CHO-）IgG体外结合从新生大鼠空肠提取的Fc受体的能力受损，除了一个案例外，在所有案例中，体内从肠腔转运到血液中的CHO- IgG量均显著减少。在存在各种糖类的情况下，未观察到正常IgG与提取的受体的结合减少。据推测，N-连接碳水化合物起到稳定IgG分子内负责与该Fc受体结合的结构的作用，可能是在CH2结构域。
