Hsien-Ya Lin, Shang-Chuen Wu, Hau-Ming Jan, Anu Paul, Victoria Ortiz, Courtney A Winters, Carter J Stowell, Vivien C Lee, Connie M Arthur
Carbohydrate-binding proteins, often called lectins, possess the unique ability to engage other macromolecules through recognition of carbohydrate structures. Among lectins, galectins have emerged as unique mammalian lectins that can possess high specificity for human carbohydrate-based blood group antigens. As such, galectins can differentiate red blood cells (RBCs) based on the blood group status of an individual. The ability of galectins to engage glycans can be studied by a wide variety of approaches. We describe herein the production of galectins and the characterization of galectin glycanbinding affinity using isothermal titration calorimetry (ITC).