1887

Abstract

Summary

A partially-purified neuraminidase from the mucinase complex of was used to prepare a specific anti-neuraminidase antiserum in rabbits. When the neutralising potency of this serum against 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 neuraminidase.

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/content/journal/jmm/10.1099/00222615-25-2-123
1988-02-01
2019-12-06
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http://instance.metastore.ingenta.com/content/journal/jmm/10.1099/00222615-25-2-123
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