Affinity of Bandeiraea (Griffonia) simplicifolia Lectin-I, Isolectin-B4 (BSI-B4) for Galα1→4Gal Ligand

A. M. Wu*, S. C. Song, J. H. Wu, E. A. Kabat

*Corresponding author for this work

Research output: Contribution to journalJournal Article peer-review

25 Scopus citations


The affinity of Bandeiraea (Griffonia) simplicifolia lectin-I isolectin B-4 (BSI-B-4) for the isomer of human blood group B active disaccharide (B, Galα1→3Gal), the Galα1→4Gal galabiose ligand, was studied by quantitative precipitin(QPA) and precipitin-inhibition assays. When human blood group B, P1 and H active glycoproteins were tested by QPA. BSI-B4 reacted strongly with both the B active glycoprotein purified from human ovarian cyst fluid and a P1 active glycoprotein isolated from sheep hydatid fluid and precipitated over 86% of the lectin nitrogen added. The P1 active glycoprotein-BSI-B4 interaction was inhibited by both Galα1→3Galα1→methyl and Galα1→4Gal disaccharide indicating that BSI-B4 is not only reacting with Gal α1→3Gal disaccharide, but also recognizing Galα1→4Gal. The galabiose sequence is frequently found in the carbohydrate chains of many glycosphingolipids located at the mammalian cell membranes such as intestinal and red blood cell membranes, for E. coli ligand binding and toxin attachment.

Original languageEnglish
Pages (from-to)814-820
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number3
StatePublished - 22 11 1995
Externally publishedYes


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