Measurement of enzymatic activity and specificity of human and avian influenza neuraminidases from whole virus by glycoarray and MALDI-TOF mass spectrometry.

Abstract

Influenza neuraminidases hydrolyze the ketosidic linkage between N-acetylneuraminic acid and its adjacent galactose residue in sialosides. This enzyme is a tetrameric protein that plays a critical role in the release of progeny virions. Several methods have been described for the determination of neuraminidase activity, usually based on colorimetric… (More)
DOI: 10.1002/cbic.201100128

Topics

7 Figures and Tables

Cite this paper

@article{Pourceau2011MeasurementOE, title={Measurement of enzymatic activity and specificity of human and avian influenza neuraminidases from whole virus by glycoarray and MALDI-TOF mass spectrometry.}, author={Gwladys Pourceau and Yann Chevolot and Alice Goudot and Fabienne Giroux and Albert Meyer and Vincent Moul{\'e}s and B. Lina and Samy Cecioni and S{\'e}bastien Vidal and Hai Yu and Xi Chen and Olivier Ferraris and J P Praly and {\'E}liane Souteyrand and Jean-Jacques Vasseur and François Morvan}, journal={Chembiochem : a European journal of chemical biology}, year={2011}, volume={12 13}, pages={2071-80} }