Affinity analysis of lectin interaction with immobilized C- and O- gylcosides studied by surface plasmon resonance assay.
J Biochem Biophys Methods
; 52(1): 11-8, 2002 Jun 28.
Article
em En
| MEDLINE
| ID: mdl-12121750
ABSTRACT
A biosensor based on the surface plasmon resonance (SPR) principle was used for kinetic analysis of lectin interactions with different immobilized saccharide structures. A novel affinity ligands beta-D-glycopyranosylmethylamines derived from common D-aldohexoses linked to the carboxymethyl dextran layer of the SPR sensor surface served for interactions with a wide range of lectins. The method of preparation and use of the beta-D-mannopyranosyl glycosylated sensor surface was described. The results of affinity analysis of lectin-ligand interactions were evaluated and compared with data obtained from measurements using commercially available p-aminophenyl alpha-D-glycopyranosides. Possible applications and advantages of C- and O-glycosylated SPR biosensors are discussed.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Biofísica
/
Técnicas Biossensoriais
/
Glicosídeos
/
Lectinas
Tipo de estudo:
Prognostic_studies
Idioma:
En
Revista:
J Biochem Biophys Methods
Ano de publicação:
2002
Tipo de documento:
Article