Bovine viral diarrhea virus: purification of surface proteins in detergent-containing buffers by fast protein liquid chromatography.
Bovine viral diarrhea virus was purified by lectin chromatography. The glycoprotein peplomers were dissociated from the virion by treatment with detergent. By a second lectin gel chromatography the glycoconjugates containing terminal galactose were prepared. In combination with lectin affinity chromatography, ion-exchange chromatography on Mono-Q in the presence of the low-UV-absorbing detergent Berol 172 proved to be a powerful technique both for analytical and preparative applications.
D002846:Chromatography, Affinity; D002852:Chromatography, Ion Exchange; D003902:Detergents; D001908:Diarrhea Viruses, Bovine Viral / Q000032:analysis* / Q000302:isolation & purification; D006023:Glycoproteins / Q000302:isolation & purification; D008565:Membrane Proteins / Q000302:isolation & purification*; D008823:Micelles; D010576:Pestivirus / Q000032:analysis*; D013501:Surface-Active Agents; D014764:Viral Proteins / Q000302:isolation & purification*; D014771:Virion / Q000032:analysis
D003902:Detergents; D006023:Glycoproteins; D008565:Membrane Proteins; D008823:Micelles; D013501:Surface-Active Agents; D014764:Viral Proteins