Blue native PAGE separation of high molecular weight protein complexes in solubilized RVFV virions.

<p>Purified virions were solubilized under native conditions by diluting virus into a buffer containing 1% Trition X-100 and removing insoluble material by centrifugation. Sample buffer containing Coomassie Blue G-250 was then added to supernatants and samples were subjected to Blue native polyacramide gel electrophoresis on 4–12% gradient gels. Native protein standards (thyroglobulin 669 kDa, apoferritin 443 kDa, beta amylase 200 kDa, alcohol dehydrogenase 150 kDa, and bovine serum albumin 66 kDa) were resolved in adjacent lanes. The position of the fastest migrating band for each protein standard is indicated on the figure. Four high molecular weight protein species were observed in solubilized virions; they are labeled I–IV on the figure.