Abstract
The observed dissociation constant κd of the lectin concanavalin A (ConA) from glycoprotein asialofetuin (ASF) changed with the concentration of inhibitory sugars. The reciprocal of κd showed a linear relationship with the reciprocal of sugar concentration. This regression line was found to be theoretically available in the analysis of the kinetics in the interaction of sugars with ConA under conditions where the binding constant Κi of sugars to ConA is more than about 333.
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CITATION STYLE
Goto, S., & Terada, H. (2002). Analysis of binding affinity of sugars to concanavalin A by surface plasmon resonance sensor BIACORE. Spectroscopy, 16(3–4), 285–288. https://doi.org/10.1155/2002/814658
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