产气荚膜梭菌的2-乙酰氨基-2-脱氧-α-D-半乳糖苷酶。一种外切糖苷酶和一种寡糖酶的分离与特性分析。
2-acetamido-2-deoxy-alpha-D-galactosidases of Clostridium perfringens. Separation and characterization of an exoglycosidase and an oligosaccharidase.
作者信息
Bell W C, Pomato N, Aminoff D
出版信息
Carbohydr Res. 1978 Mar;61:447-55. doi: 10.1016/s0008-6215(00)84504-8.
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.
通过在6.5%聚丙烯酰胺凝胶中进行电泳，已从产气荚膜梭菌培养滤液中分离出两种不同的2-乙酰氨基-2-脱氧-α-D-半乳糖苷酶。其中一种酶的迁移率为0.32--0.36（相对于溴酚蓝），被鉴定为外切糖苷酶2-乙酰氨基-2-脱氧-α-D-半乳糖苷酶。它似乎与1972年麦圭尔等人报道的酶相同。这两种酶中的第二种，相对迁移率为0.42--0.46，与1972年黄和阿米诺夫报道的寡糖酶相对应。人A型红细胞和具有A活性的水溶性糖蛋白的A特异性在与2-乙酰氨基-2-脱氧-α-D-半乳糖苷酶孵育时均被破坏，但与寡糖酶孵育时则不会。在用外切糖苷酶2-乙酰氨基-2-脱氧-α-D-半乳糖苷酶处理的A型红细胞中，如使用来自欧洲荆豆的凝集素所表明的，血型O(H)活性同时升高。
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