Lectin-dependent inhibition of antigen-antibody reaction: application for measuring 2,6-sialylated glycoforms of transferrin
Author(s) -
Koki Hoshi,
Yoshinobu Kariya,
Kiyomitsu Nara,
Hiromi Ito,
K. Matsumoto,
Masamichi Nagae,
Yoshiki Yamaguchi,
Madoka Nakajima,
M. Miyajima,
Hiroyuki Arai,
Atsushi Kuno,
Hisashi Narimatsu,
Keiro Shirotani,
Yasuhiro Hashimoto
Publication year - 2013
Publication title -
the journal of biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.28
H-Index - 115
eISSN - 1756-2651
pISSN - 0021-924X
DOI - 10.1093/jb/mvt065
Subject(s) - glycobiology , library science , government (linguistics) , medicine , political science , chemistry , biochemistry , glycan , computer science , linguistics , philosophy , glycoprotein
We developed a high-throughput Enzyme-linked immunosorbent assay (ELISA) for measuring α2,6-sialylated transferrin (Tf), based on inhibition of anti-Tf antibody binding to α2,6-sialylated Tf by a lectin, Sambucus sieboldiana Agglutinin (SSA). The inhibition was not observed with other glycoforms, such as periodate-treated, sialidase-treated and sialidase/galactosidase-treated Tf, suggesting that the assay was glycoform specific. This finding was applied to an automated latex-agglutination immunoassay, using SSA lectin as an inhibitor (SSA-ALI). The concentration of α2,6-sialylated Tf measured by SSA-ALI in human cerebrospinal fluid was correlated with that of ELISA (r2 = 0.8554), previously developed for measuring α2,6-sialylated Tf.
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