Comparison of the properties of concanavalin A and anti-alpha-D-glucose antibodies.

Concanavalin A and anti-alpha-D-glucose antibodies form precipitin complexes with antigens having alpha-D-glucose as terminal units. The sedimentation rates, molecular weights, gel electrophoretic mobilities, isoelectric points, and immunoglobulin type of Con A and alpha-Ab have been determined. The interactions of the compounds with antigens in the presence of potential inhibitors have been compared. The data show that the interaction of Con A with glucose units occurs with hydrogen bonding at hydroxyl groups at C1,3,4, and 6 and van der Waals bonding at the pyranose ring oxygen. In the alpha-Ab complex with glucose units, in addition to the above bond types, a hydrogen bond at the hydroxyl at C2 occurs and this bond is essential for interaction.