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We have recently demonstrated that the 1CF11 monoclonal antibody bound human milk lactoferrin (hLf) through the recognition of two distinct portions of the molecule, namely the N-glycan-relevant and -irrelevant structural elements. In this present study, we prepared four immunoreactive peptide fractions containing N-linked glycan from tryptic digests of reduced and alkylated hLf by using a concanavalin A lectin column and reverse-phase HPLC. Deglycosylation of these fractions and a competitive binding assay using fucosylated oligosaccharides revealed that the non-reducing terminal fucose residue in N-linked glycan(s) played a significant role in recognizing the N-glycan-relevant element in hLf by 1CF11.

bioscience, biotechnology, and biochemistry

Non-Reducing Terminal Fucose within <i>N</i>-Linked Glycan Plays a Significant Role in the Recognition of Human Milk Lactoferrin by the 1CF11 Monoclonal Antibody

Non-Reducing Terminal Fucose within N-Linked Glycan Plays a Significant Role in the Recognition of Human Milk Lactoferrin by the 1CF11 Monoclonal Antibody