Purification of detergent-extracted Sendai virus proteins by reversed-phase high-performance liquid chromatography.

Sendai virus envelope proteins were isolated by reversed-phase high-performance liquid chromatography. The F (F1 and F2, connected by disulphide bonds), M and HN proteins were extracted from purified Sendai virions with Triton X-100. After removal of the detergent from the extract with Amberlite XAD-2 and reduction of the proteins, separation was performed on a small (10-nm) and on a larger (30-nm) pore size C18 column. Proteins were eluted with a gradient of an ethanol 1-butanol mixture in 12 mM hydrochloric acid. On the 10-nm pore size column, F2 was completely recovered in pure form, whereas the recoveries of the other proteins were low (5-25%). Similar results were obtained with the 30-nm pore size column, except for protein F1 of which the yield was higher (50%).