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PMID: 5040386 Published · ppublish English Journal Article

A 2 (N2) neuraminidase of the X-7 influenza virus recombinant: determination of molecular size and subunit composition of the active unit.

Journal of virology ·Vol. 10 ·No. 1 ·1972-07-00 ·Pages 60-6

Bucher DJ, Kilbourne ED

Abstract

Neuraminidase activity of influenza virus was directly seen on sodium dodecyl sulfate polyacrylamide gels with the aid of the synthetic substrate, methoxyphenol neuraminic acid. Neuraminidase (NA) appeared as a high-molecular-weight fraction with a size in the range of 220,000 to 250,000 daltons. Isolation of this fraction from the X-7 strain of influenza virus, dissociation with sodium dodecyl sulfate, and reduction showed the presence of two polypeptides of 66,000 (NA(1)) and 58,000 (NA(2)) molecular weights in equimolar concentration. We postulate that the minimum active unit for the viral A(2) neuraminidase is a tetramer composed of two NA(1) and two NA(2) subunits.

MeSH Terms
Centrifugation, Density Gradient Chromatography Dithiothreitol Electrophoresis, Disc Genetics, Microbial Molecular Weight Neuraminidase/analysis,isolation & purification,metabolism Orthomyxoviridae/analysis,enzymology Peptides/analysis Recombination, Genetic Sodium Dodecyl Sulfate Spectrophotometry Sucrose Viral Proteins/analysis
Chemicals
Peptides Viral Proteins Sodium Dodecyl Sulfate Sucrose Neuraminidase Dithiothreitol
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Bucher D J
Kilbourne E D
References (15)
15 references, click to expand
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
DOI
10.1128/JVI.10.1.60-66.1972
Published
1972-07-00
Pages
60-6
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC356425
Subset
IM
External Links
PubMed source DOI: 10.1128/JVI.10.1.60-66.1972 PMC Full Text View journal details
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