Characterization of the major structural proteins of purified bovine viral diarrhea virus

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Abstract
Bovine viral diarrhea virus (BVDV) was concentrated and purified by a combination of ultrafiltration, hydroextraction using polyethylene glycol and affinity chromatography. A lectin fromCrotalaria juncea that has an affinity for galactose was used in the affinity chromatography. Virions of BVDV with classic envelopes were observed by electron microscopy. Four major proteins with estimated molecular weights of 75,000, 66,000, 54,000, and 26,000 were identified in sodium dodecyl sulfate—polyacrylamide gel electrophoresis slab gels. The proteins of 75,000 and 54,000 were glycoproteins as shown by staining with dansyl hydrazine.