Analysis of binding affinity of sugars to concanavalin A by surface plasmon resonance sensor BIACORE

Article type: Research Article

Authors: Goto, Satoru^; | Terada, Hiroshi

Affiliations: Faculty of Pharmaceutical Sciences, University of Tokushima, 1‐78, Shomachi, Tokushima 770‐8505, Japan | Faculty of Pharmaceutical Sciences, Tokyo University of Science, Ichigaya Funagawara‐machi, Shinjuku‐ku, Tokyo 135‐0024, Japan

Note: [] Corresponding author. Tel./Fax: +81 88 6339527; E‐mail: [email protected]‐u.ac.jp.

Abstract: The observed dissociation constant kd of the lectin concanavalin A (ConA) from glycoprotein asialofetuin (ASF) changed with the concentration of inhibitory sugars. The reciprocal of kd 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 Ki of sugars to ConA is more than about 333.

Journal: Spectroscopy, vol. 16, no. 3-4, pp. 285-288, 2002