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 language | English (US) |
---|---|
Pages (from-to) | 327-333 |
Number of pages | 7 |
Journal | Journal of Chromatography A |
Volume | 646 |
Issue number | 2 |
DOIs | |
State | Published - Sep 3 1993 |
Externally published | Yes |
ASJC Scopus subject areas
- Analytical Chemistry
- Biochemistry
- Organic Chemistry