2-acetamido-2-deoxy-alpha-D-galactosidases of Clostridium perfringens. Separation and characterization of an exoglycosidase and an oligosaccharidase.

Two distinct 2-acetamido-2-deoxy-alpha-D-galactosidases have been separated from filtrates of cultured Clostridium perfringens by electrophoresis in 6.5% poly(acrylamide) gels. One of the enzymes had a mobility of 0.32--0.36 (relative to Bromophenol Blue) and was identified as the exoglycosidase, 2-acetamido-2-deoxy-alpha-D-galactosidase. It appears to be the same enzyme as that reported in 1972 by McGuire et al. The second of the two enzymes, having a relative mobility of 0.42--0.46, corresponds to the oligosaccharidase reported in 1972 by Huang and Aminoff. The A-specificities of human type-A erythrocytes and of water-soluble glycoproteins having A-activity are both destroyed by incubation with the 2-acetamido-2-deoxy-alpha-D-galactosidase, but not on incubation with the oligosaccharidase. A concomitant rise in blood-group O(H) activity, as indicated by the use of a lectin from Ulex europeus, occurred in the A-erythrocytes treated with the exoglycosidase 2-acetamido-2-deoxy-alpha-D-galactosidase.