Isolation of Sendai virus F protein by anion-exchange high-performance liquid chromatography in the presence of Triton X-100.

Purified Sendai virions were treated with Triton X-100. The detergent extract containing the fusion protein (F) and the haemagglutinin-neuraminidase protein (HN) was subjected to anion-exchange high-performance liquid chromatography on a Mono Q (Pharmacia) column with 0.1% Triton X-100 in phosphate-buffered saline. HN was not retained by the column while elution with a salt gradient resulted in several peaks containing mainly or only F protein.