Naturally occurring glycan forms of human immunoglobulins G1 and G2.
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.
Flynn
Gregory C
GC
Department of Process and Product Development, Amgen Inc., Thousand Oaks, CA 91320, USA. gflynn@amgen.com
Chen
Xiaoyu
X
Liu
Y Diana
YD
Shah
Bhavana
B
Zhang
Zhongqi
Z
D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D006031:Glycosylation; D006801:Humans; D007074:Immunoglobulin G / Q000032:analysis / Q000737:chemistry*; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D011134:Polysaccharides / Q000032:analysis / Q000737:chemistry*
D007074:Immunoglobulin G; D011134:Polysaccharides