Optimised concentration and purification of retroviruses using membrane chromatography

The ability of an anion exchange membrane to purify a γ-retrovirus was assessed and optimised with respect to different loading and wash buffers. Recoveries of infectious virus greater than 50% were consistently obtained, while specific titre was increased up to one thousand fold when compared to th...

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Autores principales: McNally, D.J., Darling, D., Farzaneh, F., Levison, P.R., Slater, N.K.H.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2014
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4003387/
https://www.ncbi.nlm.nih.gov/pubmed/24685165
http://dx.doi.org/10.1016/j.chroma.2014.03.023
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author McNally, D.J.
Darling, D.
Farzaneh, F.
Levison, P.R.
Slater, N.K.H.
author_facet McNally, D.J.
Darling, D.
Farzaneh, F.
Levison, P.R.
Slater, N.K.H.
author_sort McNally, D.J.
collection PubMed
description The ability of an anion exchange membrane to purify a γ-retrovirus was assessed and optimised with respect to different loading and wash buffers. Recoveries of infectious virus greater than 50% were consistently obtained, while specific titre was increased up to one thousand fold when compared to the material loaded. Specific proteins removed and retained by this optimised process were identified by mass spectrometry. It was possible to successfully bind and elute the equivalent of 1.27 × 10(8) Ifu/ml of ion exchange membrane. This could then be highly concentrated, with infectious virus concentrated to a maximum of 420-fold compared to the load.
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spelling pubmed-40033872014-05-02 Optimised concentration and purification of retroviruses using membrane chromatography McNally, D.J. Darling, D. Farzaneh, F. Levison, P.R. Slater, N.K.H. J Chromatogr A Article The ability of an anion exchange membrane to purify a γ-retrovirus was assessed and optimised with respect to different loading and wash buffers. Recoveries of infectious virus greater than 50% were consistently obtained, while specific titre was increased up to one thousand fold when compared to the material loaded. Specific proteins removed and retained by this optimised process were identified by mass spectrometry. It was possible to successfully bind and elute the equivalent of 1.27 × 10(8) Ifu/ml of ion exchange membrane. This could then be highly concentrated, with infectious virus concentrated to a maximum of 420-fold compared to the load. Elsevier 2014-05-02 /pmc/articles/PMC4003387/ /pubmed/24685165 http://dx.doi.org/10.1016/j.chroma.2014.03.023 Text en © 2014 The Authors http://creativecommons.org/licenses/by/3.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Article
McNally, D.J.
Darling, D.
Farzaneh, F.
Levison, P.R.
Slater, N.K.H.
Optimised concentration and purification of retroviruses using membrane chromatography
title Optimised concentration and purification of retroviruses using membrane chromatography
title_full Optimised concentration and purification of retroviruses using membrane chromatography
title_fullStr Optimised concentration and purification of retroviruses using membrane chromatography
title_full_unstemmed Optimised concentration and purification of retroviruses using membrane chromatography
title_short Optimised concentration and purification of retroviruses using membrane chromatography
title_sort optimised concentration and purification of retroviruses using membrane chromatography
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4003387/
https://www.ncbi.nlm.nih.gov/pubmed/24685165
http://dx.doi.org/10.1016/j.chroma.2014.03.023
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