51. Simple and Rapid Detection of Glycoforms by 'Lectin Inhibition' Assay
- Author
-
Hiromi Ito, Yasuhiro Hashimoto, and Kyoka Hoshi
- Subjects
musculoskeletal diseases ,0301 basic medicine ,chemistry.chemical_classification ,Glycosylation ,biology ,Chemistry ,Sambucus sieboldiana ,Lectin ,Antigen binding ,biology.organism_classification ,Rapid detection ,eye diseases ,carbohydrates (lipids) ,stomatognathic diseases ,03 medical and health sciences ,chemistry.chemical_compound ,030104 developmental biology ,0302 clinical medicine ,Agglutinin ,stomatognathic system ,Biochemistry ,Transferrin ,biology.protein ,030217 neurology & neurosurgery - Abstract
Glycoforms are otherwise identical proteins with different glycosylation. A lectin, Sambucus sieboldiana agglutinin (SSA), specifically binds glycoforms having α2,6-sialyl residues. The binding is found to inhibit antigen-antibody reaction; e.g., SSA inhibits anti-transferrin antibody binding to α2,6-sialylated transferrin (Tf) (SSA inhibition). SSA inhibition is not observed with other Tf glycoforms, indicating that the inhibition is glycoform-specific. Here we describe the application of SSA inhibition to ELISA as a specific assay for quantifying α2,6-sialylated Tf.
- Published
- 2020