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Specificities of Ricinus communis agglutinin 120 interaction with sulfated galactose
Author(s) -
Wang Yufeng,
Yu Guangli,
Han Zhangrun,
Yang Bo,
Hu Yannan,
Zhao Xia,
Wu Jiandong,
Lv Youjing,
Chai Wengang
Publication year - 2011
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2011.10.035
Subject(s) - sulfation , ricinus , galactose , lectin , oligosaccharide , chemistry , biochemistry , agglutinin
Lectins are used extensively as research tools to detect and target specific oligosaccharide sequences. Ricinus communis agglutinin I (RCA 120 ) recognizes non‐reducing terminal β‐ d ‐galactose (Galβ) and its specificities of interactions with neutral and sialylated oligosaccharides have been well documented. Here we use carbohydrate arrays of sulfated Galβ‐containing oligosaccharide probes, prepared from marine‐derived galactans, to investigate their interactions with RCA 120 . Our results showed that RCA 120 binding to Galβ1–4 was enhanced by 2‐ O ‐ or 6‐ O ‐sulfation but abolished by 4‐ O ‐sulfation. The results were corroborated with competition experiments. Erythrina cristagalli lectin is also a Galβ‐binding protein but it cannot accommodate any sulfation on Galβ.