title: EPR and Mössbauer spectroscopy investigations on the metal ion contents of Sendai virus components.
abstract: EPR and Mössbauer spectroscopy indicate that Sendai virus contains iron ions in paramagnetic states. Spectral data show that the iron ions are in an oxidized form (Fe3+), having low and high spin states (S = 1/2 and S = 5/2). On enrichment of Sendai virus with 57Fe, the concentration of Fe3+ ions substantially increases in the virus preparations. The Fe3+ ions in the high spin state appear to be tightly bound to the virus components; they are not significantly removed by dialysis. The five main proteins separated by SDS gel electrophoresis from 57Fe-enriched Sendai virus contain the signal corresponding to the presence of Fe3+ ions in the high spin state. The concentration of Fe3+ ions is, however, about five times higher in the HN polypeptide than in the other four components. It is suggested that Fe3+ (5/2) ions might be a structural component of the Sendai virus HN polypeptide.
mesh_terms: D004578:Electron Spin Resonance Spectroscopy; D005290:Ferric Compounds / Q000032:analysis*; D006023:Glycoproteins / Q000032:analysis; D007501:Iron / Q000032:analysis*; D010222:Parainfluenza Virus 1, Human / Q000032:analysis*; D010455:Peptides / Q000032:analysis; D013057:Spectrum Analysis; D014764:Viral Proteins / Q000032:analysis*; D014771:Virion / Q000032:analysis
chemical_list: D005290:Ferric Compounds; D006023:Glycoproteins; D010455:Peptides; D014764:Viral Proteins; D007501:Iron