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The Journal of Medical Microbiology, Vol 25, Issue 2 123-128, Copyright © 1988 by Society for General Microbiology
JOURNAL ARTICLE |
D. E. Stewart-Tull and R. A. Ollar
Department of Microbiology Research Unit, Bearsden, Glasgow.
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.
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