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  • Title: Study of lectin-ganglioside interactions by high-performance liquid affinity chromatography.
    Author: Caron M, Joubert-Caron R, Cartier JR, Chadli A, Bladier D.
    Journal: J Chromatogr; 1993 Sep 03; 646(2):327-33. PubMed ID: 8408435.
    Abstract:
    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 beta-mercaptoethanol. The binding is inhibitable 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.
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