Interaction between ceruloplasmin and Sendai virus envelope components. Note III. Separation of Sendai virus envelope components by affinity chromatography.

Sendai virus envelopes solubilized by Triton X-100 at an alkaline pH were submitted to affinity chromatography on fetuin-Sepharose 4B. In the absence of Triton three groups of envelope fragments were eluted, while in the presence of detergent only two groups were separated. In both cases, envelope fragment populations eluted at low temperature contained hemagglutinin (HA), neuraminidase (N-ase) and HI-antibody blocking (HIb) activity. The populations eluted at 37 degrees C contained N-ase and HIb activity, but no HA. The populations isolated show various ratios of HA, N-ase and HIb, and have different affinities for the coupled fetuin and formolated RBC. Our data strongly suggest that binding to coupled fetuin takes place via enzymatic centres, while binding to RBC occurs via hemagglutinating centres.