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Iodination of bovine enterovirus particles revealed that during maturation, a substantial conformational change occurs among the proteins present in the procapsid.
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The differential labelling patterns suggest a substantial conformational change occurs among proteins present in the procapsid during virus maturation.
SUMMARY A bovine enterovirus (serotype VG-5-27) was iodinated with [125I] by treatment with either chloramine T or lactoperoxidase. Virus particles were degraded in steps by either procedure. Initially, RNA and VP4 were released to give an unstable component which sedimented at 75S. This was degraded eventually to slowly sedimenting mateial. When treated for less than 2 min, virus particles were iodinated in only VP1, whereas all three polypeptides were labeled in the artificial top components produced by prolonged iodination. The patternof labelling of the polypeptides in procapsids (natural empty particles) was different from that in mature virus particles.With lactoperoxidase, in particular, VP0 and VP3 were predominantly labelled in contrast to the virus particles, in which only VP1 was labelled. The observations suggest that during maturationof virus particles a substantial conformational change occurs among the proteins present in the procapsid.
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Carthew et al. (1974) studied Bovine enterovirus particles. Iodination with [125I] by chloramine T or lactoperoxidase was evaluated on Pattern of labelling of polypeptides. Iodination of bovine enterovirus particles revealed that during maturation, a substantial conformational change occurs among the proteins present in the procapsid.
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