Evaluation of fluorescence polarization method for binding study in carbohydrate-lectin interaction.
The fluorescence polarization (FP) technique was evaluated to determine molecular interaction between plant lectins and polysaccharides, yeast cells and glycopeptide after labeling the lectins with fluorescein isothiocyanate. Use of Lycoris radiata agglutinin allowed determination of the molecular interactions with large biomolecules containing mannose oligomers and polymers. Another example using a fluorescein-labeled glycopeptide also indicated that use of the FP method would allow easy observation of the molecular interactions on the quantitative base. The present technique is highly sensitive and facile because it does not require any washing procedures before measurement.
Oda
Y
Y
Faculty of Pharmaceutical Sciences, Kinki University, Higashi-osaka, Japan.
Kinoshita
M
M
Nakayama
K
K
Kakehi
K
K
D001665:Binding Sites; D050260:Carbohydrate Metabolism; D002240:Carbohydrate Sequence; D005069:Evaluation Studies as Topic; D005454:Fluorescence Polarization / Q000379:methods*; D006020:Glycopeptides / Q000378:metabolism; D037102:Lectins / Q000378:metabolism*; D008969:Molecular Sequence Data; D037121:Plant Lectins; D011134:Polysaccharides / Q000378:metabolism; D012441:Saccharomyces cerevisiae; D013025:Glycine max; D014908:Triticum
D006020:Glycopeptides; D037102:Lectins; D037121:Plant Lectins; D011134:Polysaccharides