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J. Biol. Chem., Vol. 255, Issue 24, 11737-11742, 12, 1980
GN Levy and D Aminoff
Exo-alpha-N-acetylgalactosaminidase has been purified 8000-fold from
Clostridium perfringens by gel filtration, ion exchange chromatography,
isoelectric precipitation, and negative adsorption on human O type
erythrocytes. The resulting enzyme is active at physiological pH and
temperature. Phenyl glycosides, oligosaccharides, mucins, glycolipids, and
cell membranes are substrates for this enzyme. The result of enzyme action
on blood type A erythrocytes is the loss of A activity and the simultaneous
appearance of H activity, characteristic of the O blood group type.
Polyacrylamide gel electrophoresis in sodium dodecyl sulfate demonstrates
electrophoresis in sodium dodecyl sulfate demonstrates that the blood group
A-destroying activity is distinct from the other glycosidase activities
found in C. perfringens.
Purification and properties of alpha-N-acetylgalactosaminidase from Clostridium perfringens
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