This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Bucher, D. J. Articles by Kilbourne, E. D. Search for Related Content PubMed PubMed Citation Articles by Bucher, D. J. Articles by Kilbourne, E. D.

 Previous Article  |  Next Article 

J Virol. 1972 July; 10(1): 60-66
Copyright © 1972 American Society for Microbiology. All Rights Reserved.

A₂ (N2) Neuraminidase of the X-7 Influenza Virus Recombinant: Determination of Molecular Size and Subunit Composition of the Active Unit

¹ Department of Microbiology, Mount Sinai School of Medicine, City University of New York, New York, New York 10029

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 (NA₁) and 58,000 (NA₂) molecular weights in equimolar concentration. We postulate that the minimum active unit for the viral A₂ neuraminidase is a tetramer composed of two NA₁ and two NA₂ subunits.

This article has been cited by other articles:

• De Filette, M., Martens, W., Roose, K., Deroo, T., Vervalle, F., Bentahir, M., Vandekerckhove, J., Fiers, W., Saelens, X. (2008). An Influenza A Vaccine Based on Tetrameric Ectodomain of Matrix Protein 2. J. Biol. Chem. 283: 11382-11387 [Abstract] [Full Text]