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Preparative SDS-PAGE Electrophoresis of a Recombinant Epstein-Barr Virus Encoded Protein and Its Application in Serodiagnostic Test Systems, Rev C

dard protein purification procedures. Although the urea solubilization procedure is capable of separating most of the contaminating bacterial proteins, additional purification steps were necessary to obtain the recombinant protein in such a purity that it could be used as antigen in immunological assay systems. As confirmed by extensive immunoblot analysis, size-dependent fractionation of the protein mixture by continuous elution electrophoresis turned out to be the method of choice for an efficient one-step purification of recombinant antigens to near homogeneity at a preparative scale.

As the urea within the applied sample is slowly removed during the electrophoresis procedure, the recovered protein is, in contrast to the applied protein, renatured and completely soluble in standard electrophoresis buffer. Due to incorrect refolding and precipitation within the electrophoresis column, however, a reduction in the overall yield may be observed. We have purified more than 30 recombinant antigens by continuous elution electrophoresis so far, and, following the presented protocol, the observed yields are ranging from 5 to 40% of total applied protein. Like most of our remaining recombinant antigens, expression of the recombinant p23-DHFR protein from a 250 ml bacterial culture and subsequent purification via the Model 491 prep cell provided pure antigen sufficient for coating more than 400 standard 96-well ELISA plates for optimal results.


Bibliography
Frber I et al., Serological diagnosis of infectious mononucleosis using three anti-Epstein-Barr recombinant ELISAs, J Virol Methods 42, 301307 (1993)

Gorgievski-Hrisoho M et al., Serodiagnosis of infectious mononuc
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