A bovine enterovirus (serotype VG-5-27) was grown in BHK cells and purified by sedimentation procedures. Virus particles were heated at 100° in the presence of urea-sodium dodecyl sulphate, urea or borate buffer at pH 10. Whereas complete degradation of the virus in the presence of urea-SDS showed four main polypeptides, namely VP1, VP2, VP3 and VP4, heating in the presence of urea or alkali alone resulted in the selective release of VP2 and VP4, predominantly. Electron-microscopic examination of the residual complexes showed evidence for unstable intermediate ring-like particles and also fibrous material. These complexes lacked RNA and contained mainly VP1 and VP3. We interpret the results as indicating that the polypeptide VP2 may have a specific location at the apical region of the capsid.


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