[33] α-Galactosidase

The α-galactosidase from the coffee bean is one of the few capable of hydrolyzing the nonreducing terminal α-D-galactopyranosyl residue of blood group B antigens. As part of the studies on the structure of these antigens in human erythrocytes, a method has been developed for the rapid and complete purification of the enzyme in high yields by affinity chromatography. Partial purification of the enzyme by alumina gel chromatography and Sephadex gel filtration has been described. The approach in the chapter involves the synthesis of N-acylated derivatives of, α-D-galactopyranosylamine conjugated with Sepharose. Similar derivatives of β-L-fucose, β-D-galactose and N-acetyl-β-D-glucosamine have recently been used for affinity chromatography of lectins.