Effect of Ca++ on the stability of influenza virus neuraminidase.
The neuraminidases of different strains of influenza virus varied in their stability at 37 degrees C. The enzymes of the strains with N1 neuraminidases were found to be unstable during incubation at 37 degrees C whereas the enzymes of the strains with the N2 neuraminidases were stable. Among the strains with N2 neuraminidases, the enzymes of some strains were inactivated during dialysis at 37 degrees C whereas the enzymes of others were stable. This observed loss of enzyme activity during dialysis at 37 degrees C was not restricted to a single substrate as the same loss of enzyme activity was observed irrespective of the size of the substrate used in the assay. The enzymically inactive neuraminidase was found to be non-antigenic and non-immunogenic. The inactivation of the enzyme could be prevented by the addition of Ca++ but not Mg++. Out results suggest that Ca++ is essential for the stability of the enzyme at 37 degrees C. The results would also suggest that the enzymic, antigenic and immunogenic sites are either the same or very closely situated on the surface of the neuraminidase molecule.
D000818:Animals; D000917:Antibody Formation; D002118:Calcium / Q000494:pharmacology*; D003956:Dialysis; D004355:Drug Stability; D004492:Edetic Acid / Q000494:pharmacology; D008274:Magnesium / Q000494:pharmacology; D051379:Mice; D009439:Neuraminidase / Q000276:immunology / Q000378:metabolism*; D009961:Orosomucoid / Q000378:metabolism; D009975:Orthomyxoviridae / Q000201:enzymology*; D012794:Sialic Acids / Q000378:metabolism; D013696:Temperature; D000509:alpha-Fetoproteins / Q000378:metabolism
D009961:Orosomucoid; D012794:Sialic Acids; D000509:alpha-Fetoproteins; D004492:Edetic Acid; D009439:Neuraminidase; D008274:Magnesium; D002118:Calcium