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J Chromatogr. 1993 Sep 3;646(2):327-33.

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

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  • 1Laboratoire de Biochimie et Technologie des Prot√©ines, Universit√© Paris-Nord, France.

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.

PMID:
8408435
[PubMed - indexed for MEDLINE]
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