Structural proteins from a large-plaque variant (LPV) of human parainfluenza type 3 virus were analysed by electrophoresis on Laemmli-type polyacrylamide gels. High virus concentrations were obtained by growth in BS-C-1 cells cultivated on microcarrier beads. Purification of the virus in composite equilibrium gradients of potassium tartrate:glycerol resulted in 25% recovery of input infectivity and a preparation containing <0.08% of input host cell protein and RNA. Parainfluenza type 3 virus equilibrated at a density of 1.20 g/ml in these gradients. Analysis by polyacrylamide gel electrophoresis of H-glucosamine-labelled virus taken from peak gradient fractions revealed 8 or 9 major virion peptides, ranging in mol. wt. from 17 × 10 to 125 × 10 (17K to 125K), two of which were glycoproteins. The sum of the estimated mol. wt. of these peptides, 501.5K to 570.5K, does not exceed the estimated genomic potential of other paramyxoviruses.


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