Resolution of two surface glycoproteins from human parainfluenza-3 virus by crossed immunoelectrophoresis.
The technique of two-dimensional crossed immunoelectrophoresis (CIE) was used to resolve two glycoproteins from purified human parainfluenza type 3 virus. Virus preparations were extracted with Triton X-100 and fractionated by centrifugation in a Beckman airfuge. Two immunoprecipitates were detected by CIE in the supernatant fractions, but were not found in the pellets from extracted virus. Viral glycoproteins labeled with [35S]methionine were isolated by affinity chromatography on concanavalin A (Con A) agarose columns, resolved by CIE and detected by autoradiography. Resolution of two glycoprotein peaks from as little as 4.5 micrograms of protein from extracted virus is consistent with results from polyacrylamide gel patterns showing two unique glycoproteins with molecular weights of 48 kd and 65 kd.
D002846:Chromatography, Affinity; D003208:Concanavalin A; D003378:Counterimmunoelectrophoresis; D004591:Electrophoresis, Polyacrylamide Gel; D006023:Glycoproteins / Q000302:isolation & purification*; D006801:Humans; D007122:Immunoelectrophoresis; D010224:Parainfluenza Virus 3, Human / Q000032:analysis*; D018108:Respirovirus / Q000032:analysis*; D014764:Viral Proteins / Q000302:isolation & purification*
D006023:Glycoproteins; D014764:Viral Proteins; D003208:Concanavalin A