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Purification of the structural proteins of herpes simplex virus type 1 by reverse-phase high performance liquid chromatography

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Summary

Herpes simplex virus type-1 structural proteins were solubilized in formic acid and purified by reverse-phase high performance liquid chromatography. Purified proteins have been used to prepare monospecific polyclonal antibodies which neutralized virus infectivity in vitro.

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Authors and Affiliations

  1. Department of Microbiology, University of Leeds, Leeds, U.K.

    G. R. Whittaker & D. M. Meredith

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  1. G. R. Whittaker
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  2. D. M. Meredith
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Whittaker, G.R., Meredith, D.M. Purification of the structural proteins of herpes simplex virus type 1 by reverse-phase high performance liquid chromatography. Archives of Virology 114, 271–276 (1990). https://doi.org/10.1007/BF01310757

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  • DOI: https://doi.org/10.1007/BF01310757

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