A strategy for purification and peptide sequence analysis of bovine ephemeral fever virus structural proteins. [Symposium paper]
1993
Riding, G.A. | Wang, Y. | Walker, P.J. (Commonwealth Scientific and Industrial Research Organisation, Indooroopilly (Australia). Div. of Tropical Animal Production)
A rapid and efficient procedure was devised for purification from virions of the bovine ephemeral fever virus (BEF) G, N and M2 proteins. Purified virions were treated with 0.5 percent Triton X-100 to obtain a detergent-soluble fraction from which the BEFV G protein was purified by wheat germ lectin-affinity chromatography and size-exclusion high performance liquid chromatography (SE-HPLC). The Triton X-100 insoluble fraction was treated with 0.1 percent SDS and 0.05 percent RNase A and the BEFV N and M2 proteins were purified from the soluble fraction by SE-HPLC. BEF proteins obtained by this procedure were suitable for endoproteinase digestion to generate peptides for amino acid sequence analysis. Peptides purified by 2 cycles for reverse phase HPLC produced high quality amino acid sequence which confirmed sequences previously deduced from nucleotide sequence analysis of the corresponding viral genes.
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