Isolation, Purification and Characterization of Neuraminidase.
Terminal progress rept. 1 Jul 73-30 Jun 74,
MICHIGAN UNIV ANN ARBOR
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Physical-chemical studies of neuraminidase were carried out. An investigation of the peptide nature of the subunits was undertaken by trypsin digestion of neuraminidase subunits treated with 14C-iodoacetamide. 14C-labeled cysteinyl peptides were mapped by successive chromatography and high voltage electrophoresis. Three epidemic strains of influenza virus 1957, 1960 and 1969 were compared in order to detect alterations in their fingerprint patterns which could be correlated with the antigenic differences between the strains. Alternate methods of obtaining solubilized neuraminidase were surveyed. The objective was to increase yield of enzyme from several strains of virus and to release the entire molecule without loss of a fragment. The triton X100 dissociation and dissociation methods are discussed.