Isolation of the subunits of the coronavirus envelope glycoprotein E2 by hydroxyapatite high-performance liquid chromatography.
The coronavirus glycoprotein E2, which is responsible for virus attachment to cell receptors and virus-induced cell fusion, was purified by solubilization of virions with Triton X-114 and phase fractionation. Native E2 and tryptic subunits of the glycoprotein were separated by size-exclusion high-performance liquid chromatography (HPLC). Two distinct 90 kD E2 subunits, which had identical electrophoretic mobilities when analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, were separated by hydroxyapatite HPLC in the presence of sodium dodecyl sulfate.
Ricard
C S
CS
Sturman
L S
LS
D002851:Chromatography, High Pressure Liquid; D003332:Coronaviridae / Q000032:analysis*; D017886:Durapatite; D005643:Fucose / Q000032:analysis; D006882:Hydroxyapatites; D008715:Methionine / Q000032:analysis; D008970:Molecular Weight; D012967:Sodium Dodecyl Sulfate; D014759:Viral Envelope Proteins / Q000302:isolation & purification*; D014764:Viral Proteins / Q000302:isolation & purification*
D006882:Hydroxyapatites; D014759:Viral Envelope Proteins; D014764:Viral Proteins; D005643:Fucose; D012967:Sodium Dodecyl Sulfate; D017886:Durapatite; D008715:Methionine