STUDY OF LECTIN GANGLIOSIDE INTERACTIONS BY HIGH-PERFORMANCE LIQUID AFFINITY-CHROMATOGRAPHY

被引：18

作者：

CARON, M ^{[1
]}

JOUBERTCARON, R ^{[1
]}

CARTIER, JR ^{[1
]}

CHADLI, A ^{[1
]}

BLADIER, D ^{[1
]}

机构：

[1] PASTEUR MERIEUX,F-69280 MARCY LETOILE,FRANCE

来源：

JOURNAL OF CHROMATOGRAPHY | 1993年 / 646卷 / 02期

关键词：

D O I：

10.1016/0021-9673(93)83345-S

中图分类号：

O65 [分析化学];

学科分类号：

070302 ; 081704 ;

摘要：

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.

引用

页码：327 / 333

页数：7

共 28 条

[1]

ANDO S, 1983, NEUROCHEM INT, V5, P507, DOI 10.1016/0197-0186(83)90043-8

[2] BIOTINYLATED DERIVATIVE OF A HUMAN BRAIN LECTIN - SYNTHESIS AND USE IN AFFINOBLOTTING FOR ENDOGENOUS LIGAND STUDIES [J].