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Pairing of oligosaccharides in the Fc region of immunoglobulin G
Author(s) -
Masuda Katsuyoshi,
Yamaguchi Yoshiki,
Kato Koichi,
Takahashi Noriko,
Shimada Ichio,
Arata Yoji
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01557-x
Subject(s) - fragment crystallizable region , glycosylation , chemistry , immunoglobulin g , pairing , disulfide bond , electrospray ionization , antibody , immunoglobulin fc fragments , biochemistry , mass spectrometry , chromatography , biology , receptor , immunology , physics , superconductivity , quantum mechanics
The Fc portion of immunoglobulin G (IgG) expresses paired oligosaccharides with microheterogeneities, which are associated with efficiencies of effector functions and with pathological states. A comparison of electrospray ionization mass spectrometry data obtained using a variety of Fc fragments derived from human and mouse IgG that do and do not retain the inter‐chain disulfide bridge(s) revealed that (1) the Fc portion can be asymmetric as well as symmetric with respect to glycosylation and (2) the ratios of the individual glycoforms are different from what is expected from the random pairing.