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. 1978 Aug;27(2):436–442. doi: 10.1128/jvi.27.2.436-442.1978

Chromatographic separation of the polyoma virus proteins and renaturation of the isolated VP1 major capsid protein.

J N Brady, R A Consigli
PMCID: PMC354182  PMID: 211269

Abstract

Treatment of purified polyoma virions with 6 M guanidine-hydrochloride and 0.01 M beta-mercaptoethanol resulted in the immediate loss of both hemagglutinating and plaque-forming ability. Gel filtration through Sepharose CL-6B beads allowed separation of the dimer, VP1, VP2, VP3, and histone proteins VP4-7 in highly purified form. Renaturation of the purified VP1 protein resulted in the formation of subunits that were morphologically, biophysically, and immunologically similar to native virion capsomeres.

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Selected References

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