Oligosaccharides are increasingly being recognized as important partners in glycan-lectin binding and cellular signaling. Surface plasmon resonance (SPR) is a powerful tool for the real-time study of the specific interactions between biological molecules. We have developed an efficient surface coupling chemistry to probe carbohydrate-lectin interactions in an array format using SPR imaging. The coupling agent, a thiol-functionalized perfluorophenyl azide, PFPA-MUTEG, allows the covalent attachment of carbohydrates to gold surface by way of CH insertion reactions. The SPR chips were modified with mixed SAMs of PFPA-MUTEG and MDEG before the carbohydrate ligands were arrayed and immobilized. The carbohydrate array was composed of α-1,3-α-1,6-D -mannotriose, α-1,2-D -mannobiose, D -mannose, D -glucose and D -galactose, and the binding studies were carried out using Concanavalin A, a plant lectin that exhibits mannose-binding properties. The kinetic equilibrium constant (KA), adsorption coefficient (KADS) and solution equilibrium constant (KD) were obtained for each carbohydrate at different mixed SAM composition. The SAM containing 10% MDEG showed the highest sensitivity and the least non-specific adsorption. The KADS values for mannotriose, mannobiose and mannose were measured to be 10.3 ± 1.1 x 106, 7.6 ± 1.0 x 106, 1.3 ± 1.0 x 106M-1, respectively.