Key result
Differences in the isoelectric points of some structural polypeptides were found among the three serological types of poliovirus, while those of dense particles and empty capsids were identical to standard particles.
The study identifies the isoelectric points of poliovirus polypeptides, showing differences between serotypes but identical pIs across particle types within a strain.
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pI variations may aid poliovirus serotype differentiation in lab settings; leaves open functional or immunologic implications.
The isoelectric points of polypeptides of standard and dense poliovirus particles and of empty capsids have been determined by isoelectric focusing in urea and by two-dimensional analysis. Comparing virus strains belonging to the three serological types of poliovirus, differences in the pI of some, but not all of the structural polypeptides are found. The pI of polypeptides of dense particles and of empty capsids are identical with those of standard particles. Polypeptide VPo present in empty capsids has a pI between those of VP4 and VP2.
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Hamann et al. (1978) studied Poliovirus. Isoelectric focusing and two-dimensional analysis was evaluated on Isoelectric points of polypeptides. Differences in the isoelectric points of some structural polypeptides were found among the three serological types of poliovirus, while those of dense particles and empty capsids were identical to standard particles.
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