Abstract
Corn coleoptile lectin was isolated using lactose/agarose affinity chromatograpy. The purified lectin, displaying a single band in polyacrylamide gel electrophoresis, was studied by a technique using dextran-raffinose biotinylated derivatives. Raffinose, lactose, lactulose, N-acetyl-D-galactosamine, glucose, and L-fucose were used to measure the inhibition and binding activity of the lectin. The inhibition pattern obtained agreed with previous hemagglutination inhibition data.