Differences in substrate specificity of myxovirus neuraminidases

Drzeniek, Rudolf; Gauhe, Adeline

doi:10.1016/0006-291X(70)90630-3

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Differences in substrate specificity of myxovirus neuraminidases

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Drzeniek, Rudolf
Max Planck Institute for Medical Research, Max Planck Society;

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Gauhe, Adeline
Max Planck Institute for Medical Research, Max Planck Society;

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http://www.sciencedirect.com/science/article/pii/0006291X70906303/pdf?md5=1147fa0972891b5ccdf7ba7d5e2c52f5&pid=1-s2.0-0006291X70906303-main.pdf
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Citation

Drzeniek, R., & Gauhe, A. (1970). Differences in substrate specificity of myxovirus neuraminidases. Biochemical and Biophysical Research Communications (Orlando, FL), 38(4), 651-656. doi:10.1016/0006-291X(70)90630-3.

Cite as: https://hdl.handle.net/11858/00-001M-0000-002D-7785-F

Abstract

Neuraminidase of NDV splits the (α, 2→8) linkage between two adjacent NANA molecules of disialyllactose almost as easily as the (α, 2→3) linkage between NANA and D-galactose present in 3′-sialyllactose. FPV neuraminidase, however, is barely capable of liberating NANA from disialyllactose within 15 minutes at pH 7.0, although it splits 3′-sialyllactose. These differences in substrate specificity furnish additional proof that neuraminidases of myxoviruses are coded by the viral genome. The enzymes may be used to determine the kind of linkage between NANA and the joint carbohydrate.