Isolation of the subunits of the coronavirus envelope glycoprotein E2 by hydroxyapatite high-performance liquid chromatography

J Chromatogr. 1985 Jun 19:326:191-7. doi: 10.1016/s0021-9673(01)87445-8.


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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Chromatography, High Pressure Liquid
  • Coronaviridae / analysis*
  • Durapatite
  • Fucose / analysis
  • Hydroxyapatites
  • Methionine / analysis
  • Molecular Weight
  • Sodium Dodecyl Sulfate
  • Viral Envelope Proteins / isolation & purification*
  • Viral Proteins / isolation & purification*


  • Hydroxyapatites
  • Viral Envelope Proteins
  • Viral Proteins
  • Fucose
  • Sodium Dodecyl Sulfate
  • Durapatite
  • Methionine