PURIFICATION AND CHARACTERIZATION OF THE N-TERMINAL DOMAIN OF GALECTIN-4 FROM RAT SMALL-INTESTINE

Using affinity chromatography on lactose-agarose, five beta-galactosid e binding lectins of 14 to 20 kDa were detected in the rat small intes tinal mucosa, The prominant proteins of 17 and 19 kDa were purified to homogeneity by 2D-electrophoresis. Direct IV-terminal sequencing of t he 17 kDa protein and intrachain sequencing of the 19 kDa protein prod uced sequences which are part of the N-terminal domain of the L-36/gal ectin-4. A rabbit polyclonal antibody was raised against the 19 kDa le ctin, which specifically recognized the 17 and 19 kDa lectins and dete cted a related 36 kDa protein in human undifferentiated HT29 cells.