Enzymes That Destroy Blood Group Specificity

Evidence is presented for the presence of an enzyme, α-N-acetylgalactosaminyl oligosaccharase in filtrates of Clostridium perfringens. Action of this enzyme on hog submaxillary glycoprotein results in the release of a disaccharide, characterized as 3-O-β-d-galactopyranosyl-2-acetamido-2-deoxy-d-galactose. The possibility that this oligosaccharide has resulted from transgalactosylation has been eliminated. Enzymatic treatment of several glycoproteins and blood group substances from miscellaneous sources also resulted in the production of this oligosaccharide. Since in the blood group substances N-acetylgalactosamine at the reducing end of the oligosaccharide chain is α-linked to the hydroxy amino acids of the protein core, we have here a very useful α-N-acetyl-d-galactosaminyl oligosaccharase for structural studies of the carbohydrate-protein linkage in the blood group substances and in glycoproteins.