Chromatographic separation of the polyoma virus proteins and renaturation of the isolated VP1 major capsid protein.
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.
D002213:Capsid / Q000302:isolation & purification*; D002850:Chromatography, Gel; D005455:Fluorescent Antibody Technique; D006146:Guanidines / Q000494:pharmacology; D008623:Mercaptoethanol / Q000494:pharmacology; D011120:Polyomavirus / Q000032:analysis* / Q000187:drug effects; D011487:Protein Conformation; D011489:Protein Denaturation; D014764:Viral Proteins / Q000032:analysis / Q000276:immunology / Q000302:isolation & purification*
D006146:Guanidines; D014764:Viral Proteins; D008623:Mercaptoethanol