Affinity purification of the structural proteins of a fish Rhabdovirus by the use of monoclonal antibodies.
A simple procedure for optimization of affinity chromatography is described for parallel purification of four structural proteins of viral haemorrhagic septicaemia virus. Monoclonal antibodies to be used as affinity reagents were characterized initially with respect to elution conditions by enzyme-linked immunosorbent assay. Subsequently, immobilized antibodies were tested in a microscale nonradioactive direct immunoprecipitation assay, in order to establish optimal conditions for affinity purification of the viral proteins.
Lorenzen
N
N
National Veterinary Laboratory, Arhus, Denmark.
D000818:Animals; D000911:Antibodies, Monoclonal; D002846:Chromatography, Affinity / Q000379:methods; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D011233:Precipitin Tests; D012209:Rhabdoviridae; D014337:Trout / Q000382:microbiology; D014764:Viral Proteins / Q000302:isolation & purification*
D000911:Antibodies, Monoclonal; D014764:Viral Proteins