Interaction of native and asialo rat sublingual glycoproteins with lectins

Albert M. Wu*, Anthony Herp, Shuh Chyung Song, June H. Wu, Kenneth S.S. Chang

*Corresponding author for this work

Research output: Contribution to journalJournal Article peer-review

19 Scopus citations


The binding properties of the rat sublingual glycoprotein (RSL) and its asialo product with lectins were characterized by quantitative precipitin(QPA) and precipitin inhibition(QPIA) assays. Among twenty lectins tested for QPA, native RSL reacted well only with Artocarpus integrifolia (jacalin), but weakly or not at all with the other lectins. However, its asialo product(asialo-RSL) reacted strongly with many Ga1 and Ga1NAc specific lectins- it bound best to three of the GalNAcα1→ Ser/Thr (Tn) and/or Ga1β1→ 4G1cNAc (II) active lectins [jacalin, Wistaria floribunda and Ricinus communis agglutinins] and completely precipitated each of these three lectins. Asialo-RSL also reacted well with Abrus precatorius, Glycine max, Bauhinia purpurea alba, and Maclura pomifera agglutinins and abrin-a, but not with Arachis hypogeae and Dolichos biflorus agglutinins. The interaction between asialo-RSL and lectins were inhibited by either Ga1β1 → 4G1cNAc, p-NO2-pheny1α-Ga1NAc or both. The mapping of the precipitation and inhibition profiles leads to the conclusion that the asialo rat sublingual glycoprotein provides important ligands for II (Ga1ββ1→ 4G1cNAcβ1→) and Tn(Ga1NAcα1 → Ser/Thr) active lectins.

Original languageEnglish
Pages (from-to)1841-1852
Number of pages12
JournalLife Sciences
Issue number20
StatePublished - 06 10 1995


  • asialo-RSL
  • lectin binding
  • sublingual glycoprotein


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