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

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

Research output: Contribution to journalArticle

12 Citations (Scopus)

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 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
Volume646
Issue number2
DOIs
StatePublished - Sep 3 1993
Externally publishedYes

Fingerprint

Affinity chromatography
Gangliosides
Liquid chromatography
Affinity Chromatography
Lectins
Brain
High Pressure Liquid Chromatography
Tromethamine
Mercaptoethanol
Glycolipids
Sugars
Adsorbents
Assays
Proteins
Derivatives
Liquids
saccharide-binding proteins
lysoGM1 ganglioside

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry
  • Organic Chemistry

Cite this

Study of lectin-ganglioside interactions by high-performance liquid affinity chromatography. / Caron, M.; Joubert-Caron, R.; Cartier, J. R.; Chadli, Ahmed; Bladier, D.

In: Journal of Chromatography A, Vol. 646, No. 2, 03.09.1993, p. 327-333.

Research output: Contribution to journalArticle

Caron, M. ; Joubert-Caron, R. ; Cartier, J. R. ; Chadli, Ahmed ; Bladier, D. / Study of lectin-ganglioside interactions by high-performance liquid affinity chromatography. In: Journal of Chromatography A. 1993 ; Vol. 646, No. 2. pp. 327-333.
@article{2474905d8e0741db99553eafba226daa,
title = "Study of lectin-ganglioside interactions by high-performance liquid affinity chromatography",
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 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.",
author = "M. Caron and R. Joubert-Caron and Cartier, {J. R.} and Ahmed Chadli and D. Bladier",
year = "1993",
month = "9",
day = "3",
doi = "10.1016/0021-9673(93)83345-S",
language = "English (US)",
volume = "646",
pages = "327--333",
journal = "Journal of Chromatography",
issn = "0021-9673",
publisher = "Elsevier",
number = "2",

}

TY - JOUR

T1 - Study of lectin-ganglioside interactions by high-performance liquid affinity chromatography

AU - Caron, M.

AU - Joubert-Caron, R.

AU - Cartier, J. R.

AU - Chadli, Ahmed

AU - Bladier, D.

PY - 1993/9/3

Y1 - 1993/9/3

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0027184431&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027184431&partnerID=8YFLogxK

U2 - 10.1016/0021-9673(93)83345-S

DO - 10.1016/0021-9673(93)83345-S

M3 - Article

C2 - 8408435

AN - SCOPUS:0027184431

VL - 646

SP - 327

EP - 333

JO - Journal of Chromatography

JF - Journal of Chromatography

SN - 0021-9673

IS - 2

ER -