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J Gen Virol 45 (1979), 745-749; DOI 10.1099/0022-1317-45-3-745
© 1979 Society for General Microbiology
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Biochemical Properties of Paramyxovirus Duck/Mississippi/75 Neuraminidase

Nicole Kessler and Michele Aymard

Laboratoire de Virologie WHO Collaborating Centre for Viral Reference and Research Faculte de Médecine, 8, avenue Rockefeller 69373 Lyon, Cedex 2, France

The neuraminidase activity of two strains of Duck/Mississippi/75 virus: DK/Mississippi/320 and DK/Mississippi/334 was studied. These neuraminidases hydrolyse the {alpha} 2->3 and {alpha} 2->8 ketosidic bonds of different substrates such as fetuin, N-acetyl neuramine lactose and colominic acid, but do not hydrolyse the {alpha}2->6 bonds of mucin type I and type II. The kinetic values of the neuraminidases, Michaelis constant, maximal and initial velocities and the effect of pH, temperature and detergents were also evaluated. The isolates differ mainly in the optimal pH and temperature conditions of activity. As with other paramyxovirus neuraminidases, the enzyme of DK/Mississippi/75 was destroyed by ionic but not non-ionic detergents.

Received 12 May 1979; accepted 17 July 1979.




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Copyright © 1979 by the Society for General Microbiology.