ABSTRACT
Many kinds of lectins and related molecules have been successively found in a variety of species [1]. Simultaneously, carbohydrates have been shown to play a role in a multitude of biological processes such as protein folding, clearance, cell-cell interaction, and signal transduction. To clarify the func tional roles of these molecules, we must evaluate their sugar binding proper ties and the mechanisms involved. Many assay systems for analyzing the interactions between lectin and oligosaccharides have been developed, in cluding affinity chromatography [2], microdialysis [3], microcalorimetry [4], electrophoresis [5], and nuclear magnetic resonance (NMR) [6]. How ever, because these methods usually detect the equilibrium of interactions, information about the on-and off-rate kinetics remains scarce. Recent findings have revealed that the interactions between oligosaccharides and carbohydrate-recognizing molecules are quite complicated, and those inter actions should be analyzed in more detail rather than simply observing whether binding occurs. Several important aspects of the interactions have been pointed out, including the clustering effect [7], the importance of transient interactions [8], and the effect of blood flow [9]. For the func tional analysis of an oligosaccharide in a binding assay, development of more sophisticated analytical methods is necessary.
