Department of Process and Product Development, Amgen Inc., Thousand Oaks, CA 91320, USA.
Mol Immunol. 2010 Jul;47(11-12):2074-82. doi: 10.1016/j.molimm.2010.04.006. Epub 2010 May 4.
High resolution glycan mapping was performed on human immunoglobulin G (IgG) obtained from individual healthy subjects and from a combined sample of healthy subjects. In addition to the commonly known complex glycans, a variety of minor glycans are described and quantified, including high mannose forms and several previously unreported hybrid forms. Fc specific glycan analysis was also performed through peptide mapping with LC/MS/MS. Differences in the glycan linked Fc peptide masses allowed glycan profiles to be analyzed and quantified from IgG1 and IgG2 simultaneously for each subject within the same sample. Glycan profiles differed between subtypes, with greater levels of more fully galactosylated species found on IgG1 (e.g. G2F, SG2F) than IgG2. These results also show that Gal attachment on G1F is biased to the Man (alpha1-->6) arm for IgG1 and on the Man (alpha1-->3) arm for IgG2 from individual healthy subjects.
对来自个体健康受试者和健康受试者混合样本的人免疫球蛋白 G（IgG）进行了高分辨率聚糖图谱分析。除了常见的复杂聚糖外，还描述和定量了多种少量聚糖，包括高甘露糖形式和几种以前未报道的杂合形式。通过 LC/MS/MS 的肽图谱分析也进行了 Fc 特异性聚糖分析。连接 Fc 的聚糖肽质量的差异允许对同一样本中每个受试者的 IgG1 和 IgG2 同时进行聚糖谱分析和定量。聚糖谱在亚型之间存在差异，在 IgG1（例如 G2F、SG2F）上发现了更多完全半乳糖化的物种，其水平高于 IgG2。这些结果还表明，Gal 附着在 IgG1 的 Man（alpha1-->6）臂上和 IgG2 的 Man（alpha1-->3）臂上偏向于个体健康受试者。
