Separation of the integral membrane glycoproteins E1 and E2 of Semliki Forest virus by affinity chromatography on concanavalin A-Sepharose.
The membrane glycoproteins E1 and E2 of Semliki Forest virus are of about equal size but can be separated from each other by affinity chromatography on a concanavalin A-Sepharose column in the presence of sodium dodecyl sulfate. The E1 protein eluted like glycopeptides containing two peripheral sugar branches composed of N-acetylglucosamine, mannose, galactose and sialic acid. The E2 eluted like glycopeptides containing only N-acetylglucosamine and mannose.
D002250:Carbon Radioisotopes; D002846:Chromatography, Affinity / Q000379:methods; D003208:Concanavalin A; D005690:Galactose; D006020:Glycopeptides / Q000032:analysis; D006023:Glycoproteins / Q000302:isolation & purification*; D007553:Isotope Labeling; D008358:Mannose; D008565:Membrane Proteins / Q000302:isolation & purification*; D012672:Semliki forest virus / Q000032:analysis*; D014316:Tritium; D014764:Viral Proteins / Q000302:isolation & purification*
D002250:Carbon Radioisotopes; D006020:Glycopeptides; D006023:Glycoproteins; D008565:Membrane Proteins; D014764:Viral Proteins; D014316:Tritium; D003208:Concanavalin A; D008358:Mannose; D005690:Galactose