Stewart-Tull D E, Ollar R A
Department of Microbiology Research Unit, Bearsden, Glasgow.
J Med Microbiol. 1988 Feb;25(2):123-8. doi: 10.1099/00222615-25-2-123.
A partially-purified neuraminidase from the mucinase complex of Vibrio cholerae was used to prepare a specific anti-neuraminidase antiserum in rabbits. When the neutralising potency of this serum against V. cholerae neuraminidase was assessed in conventional tests, the enzymic activity, as measured by thiobarbituric acid, methoxyphenol-neuraminate and goblet-cell assays, apparently increased. These results are attributable to the presence of a sialylated glycoprotein substrate and small amounts of sialidase in the crude antiserum. However, a twice-purified DEAE-IgG fraction of the antiserum neutralised the enzymic activity of the V. cholerae neuraminidase.
从霍乱弧菌粘蛋白酶复合物中提取的部分纯化神经氨酸酶，被用于在兔子体内制备特异性抗神经氨酸酶抗血清。当通过常规试验评估该血清对霍乱弧菌神经氨酸酶的中和效力时，用硫代巴比妥酸、甲氧基苯酚 - 神经氨酸酯和杯状细胞测定法测得的酶活性明显增加。这些结果归因于粗抗血清中存在唾液酸化糖蛋白底物和少量唾液酸酶。然而，抗血清经两次纯化的DEAE - IgG组分可中和霍乱弧菌神经氨酸酶的酶活性。
