Study of lectin-ganglioside interactions by high-performance liquid affinity chromatography

M. Caron, R. Joubert-Caron, J. R. Cartier, A. Chadli, D. Bladier

Research output: Contribution to journalArticlepeer-review

15 Scopus citations


A high-performance affinity column containing immobilized modified GM1 (lyso-GM1) was used to study the binding of an endogenous human brain lectin (HBL) in comparison with other carbohydrate-binding proteins. The proteins are previously converted into biotinylated derivatives. Detection of biotinylated proteins in the eluates by a microtitre plate assay ensures good sensitivity. The maximum binding capacity of the adsorbent for HBL is obtained in Tris buffer supplemented with β-mercaptoethanol. The binding is inhabitable by specific sugar. It is concluded that the use of immobilized glycolipids in analytical high-performance liquid affinity chromatographic methods may serve as models in the study of interactions between gangliosides and carbohydrate-binding proteins.

Original languageEnglish (US)
Pages (from-to)327-333
Number of pages7
JournalJournal of Chromatography A
Issue number2
StatePublished - Sep 3 1993
Externally publishedYes

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry
  • Organic Chemistry


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