Levy G N, Aminoff D
J Biol Chem. 1980 Dec 25;255(24):11737-42.
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.
已通过凝胶过滤、离子交换色谱、等电沉淀以及在人O型红细胞上的负吸附从产气荚膜梭菌中纯化出α-N-乙酰半乳糖苷外切酶8000倍。所得酶在生理pH值和温度下具有活性。苯基糖苷、寡糖、粘蛋白、糖脂和细胞膜都是该酶的底物。该酶作用于A型血红细胞的结果是A活性丧失，同时出现O血型特有的H活性。十二烷基硫酸钠聚丙烯酰胺凝胶电泳表明，破坏血型A的活性与产气荚膜梭菌中发现的其他糖苷酶活性不同。
