Endotoxin-free purification for the isolation of Bovine Viral Diarrhoea Virus E2 protein from insoluble inclusion body aggregatesExport / Share Share this record       Export this recordPlumX View Altmetrics View AltmetricsCavallaro, A. S., Mahony, D., Commins, M., Mahony, T. J. and Mitter, N. (2011) Endotoxin-free purification for the isolation of Bovine Viral Diarrhoea Virus E2 protein from insoluble inclusion body aggregates. Microbial Cell Factories, 10 (1). p. 57. ISSN 1475-2859 Full text not currently attached. Access may be available via the Publisher's website or OpenAccess link. Article Link: http://doi.org/10.1186/1475-2859-10-57 Publisher URL: https://doi.org/10.1186/1475-2859-10-57 AbstractProtein expression in Escherichia coli may result in the recombinant protein being expressed as insoluble inclusion bodies. In addition, proteins purified from E. coli contain endotoxins which need to be removed for in vivo applications. The structural protein, E2, from Bovine Viral Diarrhoea Virus (BVDV) is a major immunogenic determinant, and is an ideal candidate as a subunit vaccine. The E2 protein contains 17 cysteine residues creating difficulties in E. coli expression. In this report we outline a procedure for successfully producing soluble and endotoxin-free BVDV E2 protein from inclusion bodies (IB).
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