Involvement of Both the N-Glycan-relevant and N-Glycan-irrelevant Structural Elements in the Recognition of Human Milk Lactoferrin by the 1CF11 Monoclonal Antibody | Zendy

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

Open Access

Involvement of Both the N-Glycan-relevant and N-Glycan-irrelevant Structural Elements in the Recognition of Human Milk Lactoferrin by the 1CF11 Monoclonal Antibody

Author(s) -

Shinichi FUKAYA,

Chisato SHINODA,

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.100405

Subject(s) - glycan , epitope , lactoferrin , monoclonal antibody , glycoprotein , chemistry , biochemistry , trypsin , antibody , biology , enzyme , immunology

Monoclonal antibody 1CF11 has been suggested to specifically recognize a certain carbohydrate epitope shared by glycoproteins in human external secretions. We examined the effect of cleaving the polypeptide backbone and removing N-linked oligosaccharides on the reactivity with 1CF11 of human milk lactoferrin (hLf) to elucidate the structural features of the 1CF11 epitope. We reveal by treating hLF with trypsin and/or N-glycosidase that both the N-glycan-relevant and N-glycan-irrelevant structural elements were involved in the recognition of hLf by 1CF11.

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