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.
D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D015707:HN Protein; D017830:Octoxynol; D010222:Parainfluenza Virus 1, Human / Q000032:analysis*; D011092:Polyethylene Glycols; D014759:Viral Envelope Proteins / Q000302:isolation & purification; D014760:Viral Fusion Proteins; D014764:Viral Proteins / Q000302:isolation & purification*; D014771:Virion / Q000032:analysis
D015707:HN Protein; D014759:Viral Envelope Proteins; D014760:Viral Fusion Proteins; D014764:Viral Proteins; D011092:Polyethylene Glycols; D017830:Octoxynol