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

Shinichi FUKAYA | Zendy; Tomio Yabe | Zendy; Yoshihiro Kanamaru | Zendy

Open Access

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

Author(s) -

Shinichi FUKAYA,

Tomio Yabe,

Yoshihiro Kanamaru

Publication year - 2010

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.100436

Subject(s) - glycan , fucose , lactoferrin , monoclonal antibody , chemistry , concanavalin a , biochemistry , peptide , glycosylation , residue (chemistry) , lectin , antibody , microbiology and biotechnology , glycoprotein , biology , in vitro , immunology

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.

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