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The structural analysis of the O‐glycans of the jacalin‐bound rabbit immunoglobulin G
Author(s) -
Kabir S.,
Gerwig G. J.
Publication year - 1997
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549700203201
Subject(s) - jacalin , glycan , chemistry , sialoglycoprotein , antibody , neuraminic acid , immunoglobulin g , biochemistry , lectin , chromatography , sialic acid , glycoprotein , microbiology and biotechnology , biology , immunology
Rabbit immunoglobulin G (IgG) is a sialoglycoprotein (2.4% carbohydrate), containing both N‐glycolyl (Neu5Gc) and N‐acetyl (Neu5Ac) neuraminic acids in a ratio of 87:13. A small fraction of rabbit IgG (about 25% of total IgG) bound to jacalin as demonstrated by affinity chromatography. The jacalin‐bound rabbit IgG contained O‐linked glycans which were liberated from the protein by β‐elimination and isolated. Two O‐glycan structures were determined by 1H‐NMR spectroscopy, as being Neu5Gc(α2‐3)‐Gal (β31‐3)‐GalNAc‐ol and Neu5Ac(α2‐3)‐Gal(β1‐3)‐GalNAc‐ol in a ratio of 83…n17.