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  Differences in substrate specificity of myxovirus neuraminidases

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.

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BiochemBiophysResComm_38_1969_651.pdf (Any fulltext), 260KB
 
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 Creators:
Drzeniek, Rudolf1, Author              
Gauhe, Adeline1, Author              
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1Max Planck Institute for Medical Research, Max Planck Society, ou_1125545              

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 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.

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Language(s): eng - English
 Dates: 1969-12-082004-12-081970-02-20
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/0006-291X(70)90630-3
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Title: Biochemical and Biophysical Research Communications (Orlando, FL)
  Other : Biochem Biophys Res Commun
Source Genre: Journal
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Publ. Info: Orlando, Fla. : Academic Press
Pages: - Volume / Issue: 38 (4) Sequence Number: - Start / End Page: 651 - 656 Identifier: ISSN: 0006-291X
CoNE: https://pure.mpg.de/cone/journals/resource/954922652205