免疫球蛋白IgG的n -糖基化及其临床意义

M. Papakonstantinou, G. Dryllis, M. Efstathopoulou, Dimitra Vlachopanou, Michalis Kechriotis, S. Valsami
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引用次数: 4

摘要

IgG免疫球蛋白是人体内主要的免疫球蛋白。他们有最长的半场时间,也是所有比赛中被研究最多的。Ag结合后,有一个信号通过Fc区。免疫球蛋白的翻译后修饰主要包括n -糖基化,主要是IgG修饰。igg代表抗体,它是免疫的介质,对抗细胞外细菌和毒素。Fcγ受体存在于所有造血细胞中。受体的细胞外部分在氨基酸序列上具有高度的同源性。单克隆抗体可以区分它们。除了核酸、蛋白质和脂质外,糖也是动物系统的基本组成部分。与基因组学和蛋白质组学的进展相比,糖科学的研究还处于起步阶段
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N-Glycosylation of IgG Immunoglobulin and its clinical significance
The IgG immunoglobulins are the main immunoglobulins in human beings. They have the longest half time and are the most studied of all. After the Ag binding, there is a signaling through the Fc region. The post translational modification of the immunoglobulin mainly includes the N-Glycosylation and mostly the IgG one. The IgGs represent the antibodies, which are the mediators of the immunity, against extracellular bacteria and toxins. The Fcγ receptors exist in all hemopeitic cells. The extracellular parts of the receptors show high grade of homology in their amino acid sequences. Monoclonal antibodies can distinguish them. In addition to nucleic acids, proteins and lipids, sugars are also fundamental components of animal systems. Compared with advances in genomics and proteomics, the study of glycoscience is under
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